| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-122SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB110-67828 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB600-1384SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB500-201SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-2331SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | BC100-494SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-417SS | |||
![<b>Genetic Strategies Validation. </b>Reduction of HIF-2alpha levels leads to protection in UV-triggered apoptosis, but not for apoptosis caused by glucose and serum starvation in 786-O cells. Parental 786-O or those either stably expressing wild-type VHLp19 or stably infected with a control vector (pSuperRetro) or a pool of two HIF-2alpha shRNAs vectors [21] were grown to confluence and lysed. Cell alpha-tubulin.](http://images.novusbio.com/fullsize/HIF-2-alpha-EPAS1-Antibody-Knockdown-Validated-NB100-122-img0033.jpg)
![Western Blot: Rabbit Polyclonal HIF-2 alpha/EPAS1 Antibody [NB100-122] - Analysis of HIF-2 alpha/EPAS1 antibody on mouse liver nuclear extracts. Image from a verified customer review.](http://images.novusbio.com/fullsize/antibody/nb100-122_rabbit-polyclonal-hif-2-alpha-epas1-antibody-western-blot-222024141448..jpg)
![Immunocytochemistry/ Immunofluorescence: HIF-2 alpha/EPAS1 Antibody - BSA Free [NB100-122] - Muscle repair following eccentric contraction–induced injury is concomitant with dynamic alterations of HIF2A & HIF1A expression in SCs.(A–C) Representative images of EDL myofibers from injured muscles at various time points (n >50 myofibers from 3 mice/group/time point) & stained for Pax7, DAPI, & EdU (A), HIF2A (B), or HIF1A (C). Scale bars: 20 μm. Arrowheads indicate SCs. (D) Number of Pax7+ SCs per myofiber at various time points. (E) Percentage of EdU+ SCs at various time points. (F) Percentage of HIF2A+ SCs at various time points. (G) Percentage of HIF1A+ SCs at various time points. Data represent the mean ± SEM. Image collected & cropped by CiteAb from the following publication (//www.jci.org/articles/view/96208), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-122_rabbit-polyclonal-hif-2-alpha-epas1-antibody-31020241535648.jpg)
![Immunocytochemistry/ Immunofluorescence: HIF-2 alpha/EPAS1 Antibody - BSA Free [NB100-122] - Genetic ablation of HIF2A in QSCs leads to transient activation, proliferation, & differentiation of SCs.(B) Representative images of myofibers from SC-HIF2AKO mice & control littermates (n >50 myofibers from 5 mice/group; 10 dpr). Immunofluorescence of Pax7 (red), HIF2A (green), MyoD (purple), & DAPI (blue) staining revealed HIF2A–MyoD+ & HIF2A+MyoD– SCs (arrowheads) in SC-HIF2AKO & control mice, respectively. Scale bar: 10 μm. Image collected & cropped by CiteAb from following publication (//www.jci.org/articles/view/96208), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-122_rabbit-polyclonal-hif-2-alpha-epas1-antibody-3102024153569.jpg)
![Immunocytochemistry/ Immunofluorescence: HIF-2 alpha/EPAS1 Antibody - BSA Free [NB100-122] - EpEX & EpCAM activate a STAT3-HIF2 alpha signal for EpEX/EpCAM-mediated iPSC formation.(A) iPSCs were infected with two different EpCAM shRNAs (two clones, #1 & #2). The protein expressions of EpCAM & HIF2 alpha were detected by Western blotting. (B) MEFs were stimulated by EpEX (1 μg/mL) at the indicated times. Nuclear-translocation was detected with a specific antibody against HIF2 alpha (n = 3). (C) Immunofluorescence staining was performed to detect subcellular localization of HIF2 alpha . Nuclei were stained with DAPI. Scale bar: 10 μm. (D) MEFs were treated with STAT3 inhibitor (WP1066, 10 μM), & then stimulated with EpEX for 30 min. The nuclear-translocation of HIF2 alpha was detected by Western blotting with anti-HIF2 alpha antibody (n = 3). (E) iPSC morphology was observed at day 20 after induction. Reprogramming of Oct4-GFP MEFs was induced by transfection of OSKM, OE + EpEX, & KE + EpEX with or without STAT3 inhibitor WP1066, or HIF2 alpha shRNA (n = 3). Scale bar: 50 μm. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/srep41852), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-122_rabbit-polyclonal-hif-2-alpha-epas1-antibody-310202415532070.jpg)
![Gel Super Shift Assays: HIF-2 alpha/EPAS1 Antibody - BSA Free [NB100-122] - Manipulation of DNA methylation at HRE sequences alters HIF binding. (A) The Hypoxia Response Element (HRE) contains a CpG site that can be methylated which prevents HIF1 & HIF2 binding in vitro. EMSA of in vitro–translated HIF1 & HIF2 binding to 32P-labelled unmethylated & methylated HRE probes. Competition with 250X molar excess of unlabelled/unmethylated HRE probe (lanes 3, 7,12, 16) or unlabelled control HRE-free probe (lanes 4, 8, 13, 17). HIF1 & HIF2 complexes bound to unmethylated HRE or methylated HRE supershifted with anti-HIF1 alpha (lanes 9 & 18) & anti-HIF2 alpha (lanes 5 & 14). (B) RCC4-VHL cells were grown in normoxia (NT) or treated with 25 µM decitabine (5aza) or grown in hypoxia (1%) for 48 hrs & with the addition of 25 µM decitabine (1% + 5aza). QPCR was performed using primers specific to VEGF, uPAR, TGF alpha , GUS, U1AsnRNP1. Samples were normalised to relative expression of the housekeeping gene, ACTIN. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-018-21524-5), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-122_rabbit-polyclonal-hif-2-alpha-epas1-antibody-310202415532046.jpg)
![Immunocytochemistry/ Immunofluorescence: HIF-2 alpha/EPAS1 Antibody - BSA Free [NB100-122] - HIF-1 alpha /2 alpha expression in myeloid-specific KO mice targeting the HIF pathway. (A) Images of the colon of wild-type (WT), myeloid-specific Hif-1a KO (hMRP8 Hif-1a KO) or von Hippel Lindau (Vhl) KO (hMRP8 Vhl KO) mice, immunostained for MRP8 (green) & the DNA-binding regions of Hif-1a mRNA (red). Mice were fed with 5% DSS for 4 days prior to immunostaining analyses. Note that there were no MRP8-positive cells that were positive for Hif-1a mRNA in hMRP8 Hif-1a KO (middle column) mice, but we observed many cells that were double positive for MRP8 & Hif-1a mRNA in hMRP8 Vhl KO mice (right column). (B) Images of the colon of hMRP8 Vhl KO mice fed with 5% DSS as in A, immunostained for MRP8 (green) & HIF-1 alpha (red, upper row) or HIF-2 alpha (red, bottom row). DAPI-stained nuclei are shown in blue. White boxes in A & B indicate the regions magnified in the lower or right images, respectively. Yellow arrowheads in A & B indicate cells positive for both markers. Scale bars: 100 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29967068), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-122_rabbit-polyclonal-hif-2-alpha-epas1-antibody-31020241612668.jpg)
![Immunocytochemistry/ Immunofluorescence: HIF-2 alpha/EPAS1 Antibody - BSA Free [NB100-122] - HIF2 alpha stabilization results in exocrine cell atrophy & expansion of duct-like tubular structures. (A) Body weight (left panel), pancreas weight (middle panel) & body/pancreas weight ratio (right panel) in Pdx1-Cre;HIF2dPA & control mice at 2 & 8 weeks of age. Data are presented as mean ± SD. (B) HIF2 alpha accumulation in Pdx1-Cre;HIF2dPA analyzed by Western blot with anti-HA antibody. Two independent two-week-old control & mutant mice are shown. beta -actin protein was used for loading control. Full-length blots are presented in Supplementary Fig. 2. (D) Immunofluorescence analysis of HIF2 alpha in two-week-old control pancreata. Endogenous HIF2 alpha expression is observed in islets (marked by an white asterisk) but not in exocrine tissue. (D) Robust HIF2 alpha accumulation in the pancreas of two-week-old Pdx1-Cre;HIF2dPA mice. Hematoxylin/Eosin-stained pancreatic sections from P0 (E,F), two- (I,J) & eight-week-old (M,N) Pdx1-Cre;HIF2dPA & control mice. Inset in N shows an area with adipose tissue in Pdx1-Cre;HIF2dPA pancreata. Immunofluorescence of amylase & KRT19 shows no differences between Pdx1-Cre;HIF2dPA & control mice at P0 (G,H). Duct-like tubular structures & loss of amylase immunoreactivity in two- (K,L) & eight-week-old (O,P) Pdx1-Cre;HIF2dPA mice compared to control mice. Note areas with normal acini in 8-week-old Pdx1-Cre;HIF2dPA mice (white asterisk in O). Insets in (H,L & P) show higher magnification pictures. DAPI staining is shown in blue in (C,D,G,H,K,L,O & P). Scale bars = 50 µm for (C,D); 100 µm for (E–P). ***P 50 myofibers from n = 3 mice) showing that nmGFP+ QSCs were pimonidazole+. Scale bars: 50 μm & 10 μm (insets). Inset images show that pimonidazole signals were relatively enriched in the cytoplasm of QSCs. Arrowheads indicate a QSC; asterisks indicate a myonucleus. (B) Percentage of pimonidazole+ QSCs. (C) Timeline of in vivo CCI-103F labeling in C57BL/6 mice & representative images of uninjured/resting EDL myofibers (n >50 myofibers from 3 mice) showing that nmGFP+ QSCs were CCI-103F+. Arrowheads indicate a QSC; asterisks indicate a myonucleus. Scale bar: 20 μm. (D) Percentage of CCI-103F+ QSCs. (E & F) Representative images of uninjured/resting EDL myofibers from C57BL/6 mice (n >50 myofibers from 6 mice/group) showing that most QSCs were HIF2A+, but HIF1A–. Scale bars: 10 μm. (G) Percentage of HIF1A+ & HIF2A+ QSCs. Data represent the mean ± SEM. Image collected & cropped by CiteAb from the following publication (//www.jci.org/articles/view/96208), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-122_rabbit-polyclonal-hif-2-alpha-epas1-antibody-310202415541931.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - MCDK cells induced with C22H24N2O8 to control the expression of the gene of interest. Beta-actin blocking confirms the albumin assay showing that an equal amount of lysate was loaded in each lane.](http://images.novusbio.com/fullsize/beta-Actin-Antibody-AC-15-Western-Blot-NB600-501-img0023.jpg "Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - MCDK cells induced with C22H24N2O8 to control the expression of the gene of interest. Beta-actin blocking confirms the albumin assay showing that an equal amount of lysate was loaded in each lane.")
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - Beta-Actin expression in Fibroblast Hs68 cell lysate using anti-beta-Actin antibody. Image from verified customer review.](http://images.novusbio.com/fullsize/beta-Actin-Antibody-AC-15-Western-Blot-NB600-501-img0026.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - Cell line lysates were separated on SDS-PAGE and probed with 1:5000 Monoclonal Anti-beta-Actin Clone: AC-15 . The antibody was developed using Goat Anti-Mouse IgG-Peroxidase and a chemiluminescent substrate.Lanes: 1. HeLa, 2. JURKAT, 3. COS7, 4. NIH-3T3, 5. PC-12, 6. RAT2, 7.CHO, 8. MDBK, 9. MDCK](http://images.novusbio.com/fullsize/beta-Actin-Antibody-AC-15-Western-Blot-NB600-501-img0040.jpg)
![Immunocytochemistry/Immunofluorescence: beta-Actin Antibody (AC-15) [NB600-501] - Analysis of beta-Actin antibody on mouse fibroblasts. Image from verified customer review.](http://images.novusbio.com/fullsize/beta-Actin-Antibody-AC-15-Immunocytochemistry-Immunofluorescence-NB600-501-img0038.jpg)
![Immunohistochemistry: beta-Actin Antibody (AC-15) [NB600-501] - Staining of formalin-fixed, paraffin-embedded human heart sections with 1:1000 Monoclonal Anti-beta-Actin Clone: AC-15.](http://images.novusbio.com/fullsize/beta-Actin-Antibody-AC-15-Immunohistochemistry-NB600-501-img0039.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - Analysis of beta-Actin in bovine whole skeletal muscle lysate. Image from verified customer review.](http://images.novusbio.com/fullsize/beta-Actin-Antibody-AC-15-Western-Blot-NB600-501-img0016.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - Whole cell extract of human fibroblasts was separated on SDS-PAGE and blotted with Monoclonal Anti-beta-Actin. The antibody was developed with Goat Anti-Mouse IgG, Peroxidase conjugate and AEC substrate. Lanes A: Antibody dilution 1:5,000 B: Negative control (only secondary antibody).](http://images.novusbio.com/fullsize/beta-Actin-Antibody-AC-15-Western-Blot-NB600-501-img0022.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - beta-Actin expression in human glioma cells using anti-beta-Actin antibody. Image from verified customer review.](http://images.novusbio.com/fullsize/beta-Actin-Antibody-AC-15-Western-Blot-NB600-501-img0027.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - HEK293T cells transfected with Niaph virus Matrix Protein, expression 24h later. This image was submitted via customer review.](http://images.novusbio.com/fullsize/beta-Actin-Antibody-AC-15-Western-Blot-NB600-501-img0033.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - MMP-11 expression in oral cancer cell lines and the MMP-11 knockdown in SCC9 cells reduce cell migration. Western blot analysis showing the expression of MMP-11 protein in five oral cancer cell lines. Beta-Actin is included as a loading control. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0113129), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/beta-Actin-Antibody-AC-15-Western-Blot-NB600-501-img0034.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - HSP90 and HSP70 interact with PABPN1. Interaction of PABPN1 with HSP90. Lysates from HEK293 cells transfected with Flag-HSP90 and GFP-tagged A17-PABPN1 were immunoprecipitated with an anti-Flag antibody. Immunoprecipitates (IP) were analyzed by Western blot (IB).Beta-Actin is included as a loading control. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0138936), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/beta-Actin-Antibody-AC-15-Western-Blot-NB600-501-img0035.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - GFAP and IL-6 are elevated in cultures of spinal cord compared to cortical astrocytes. ((G, H) Analysis of protein homogenates from brain or spinal cord astrocyte cultures also demonstrated higher levels of GFAP expression, but no differences in ALDH1L1. Beta-Actin is included as a loading control. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0180697), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/beta-Actin-Antibody-AC-15-Western-Blot-NB600-501-img0037.jpg)
![Immunocytochemistry/Immunofluorescence: beta-Actin Antibody (AC-15) [NB600-501] - Cultured FS-11 human fibroblast cell line stained using Monoclonal Anti-Beta-Actin, Clone No. AC-15 (NB600-501).](http://images.novusbio.com/fullsize/beta-Actin-Antibody-AC-15-Immunocytochemistry-Immunofluorescence-NB600-501-img0019.jpg)
![Immunocytochemistry/Immunofluorescence: beta-Actin Antibody (AC-15) [NB600-501] - HS-68 cells.](http://images.novusbio.com/fullsize/beta-Actin-Antibody-AC-15-Immunocytochemistry-Immunofluorescence-NB600-501-img0024.jpg)
![Simple Western: beta-Actin Antibody (AC-15) [NB600-501] - Analysis using the HRP conjugate of NB600-501. Electropherogram image(s) of corresponding Simple Western lane view. Beta-Actin antibody was used at 1:500 dilution on Hela, MCF-7, SH-SY5Y, & Jurkat lysate(s).](http://images.novusbio.com/fullsize/beta-Actin-Antibody-AC-15-Simple-Western-NB600-501-img0029.jpg)
![Simple Western: beta-Actin Antibody (AC-15) [NB600-501] - Analysis using the HRP conjugate of NB600-501. Image shows a specific band for Beta-Actin in 0.2 mg/mL of Hela, MCF-7, SH-SY5Y, & Jurkat lysate(s). This experiment was performed under reducing conditions using the 12-230 kDa separation system. * Non-specific interaction with the 230 kDa Simple Western standard may be seen with this antibody.](http://images.novusbio.com/fullsize/beta-Actin-Antibody-AC-15-Simple-Western-NB600-501-img0041.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - Effect of IFN-gamma pretreatment on carfilzomib sensitivity of H727 (a) & H23 (b) cells. IFN-gamma (150 U⋅ml−1) pretreatment for 24 h led to increased expression (left panel) & activity (middle panel) of proteasome immuno-subunits, & sensitized H727 cells to Cfz, while desensitizing H23 cells towards Cfz. The IC50 values displayed a statistically significant difference between IFN-gamma -pretreated cells & vehicle control (P value 0.1, n = 3). (c) Immunoblotting results showing no detectable expression of P-glycoprotein (P-gp) in H727 cells. DLD-1 cells with acquired Cfz resistance via P-gp upregulation (DLD-1/CfzR) were used as a positive control. (d) The co-treatment of reversin-121 (7.5 µM, P-gp inhibitor) did not affect the sensitivity of H727 cells to Cfz. The IC50 values did not show statistically significant difference between in the presence & absence of reversin-121 (Student’s t-test). (e) The levels of remaining Cfz in culture media were comparable between H727 & H23 cells (no statistically significant differences, t-tests the Holm-Sidak method to correct for multiple comparisons with alpha = 0.05). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30858500), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-501_mouse-monoclonal-beta-actin-antibody-ac-15-3102024161895.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - (a) Immunoblots showing the expression of cP & iP catalytic subunits in H727 & H23 cells. Immunoblots for additional cell lines displaying differential expression of proteasome catalytic subunits are presented in Supplementary Fig. S2. (b) Heat map displaying differential proteasome activity profiles in H727 & H23 cell lines. Purified human 20S cP & iP were used as controls for individual subunits: 20S cP for beta 5 & beta 1 & 20S iP for beta 5i & beta 1i. The numbers represent hydrolysis rates of respective substrates (RFU/min, mean values derived from three technical replicates) & were converted to color format & clustered by using the program “R” (//www.R-project.org). (c) Remaining catalytic activities of individual proteasome subunits in H727 & H23 cells 4 h after treatment with 20 nM of carfilzomib (left panel) or 20 nM bortezomib (right panel). Data are presented as mean ± SD derived from three technical replicates. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30858500), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-501_mouse-monoclonal-beta-actin-antibody-ac-15-31020241616080.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - Effects of insulin on AKT & ERK phosphorylation & cell viability in primary human pancreatic duct cells. Phosphorylated AKT & ERK were measured in primary pancreatic exocrine cultures treated with the indicated concentrations of insulin for 5 minutes (A, B) & 24 hours (C, D) (n =3-4) Fold refers to the fold change of sample relative to control at the same time point. (E) Quantification of automated cell-counting studies employing live-cell imaging of Hoechst-labeled cell cultures over 60 hours. (n =3). (F) Quantification of proliferation by BrdU staining of treated relative to untreated over 3 days (n =4). (G) Quantification of the average number of dying/dead treated cells, propidium iodide (PI) labeled, over 60 hours relative to non-treated cells. (n =3). (H) Human exocrine cells were exposed to 0, 0.2, 2, 20, 200 nM insulin for 3 days. Bright-field images are representative of 3 cultures. (I) Effects of inhibition of RAF1/ERK signalling on PI incorporation with 10 μM GW5074 or AKT signalling with 100 nM Akti1/2 on human primary pancreatic exocrine cell viability (n =3). SF denotes serum free. Repeated Measures ANOVA analyses with Bonferroni’s post-test were performed. *Represents statistical significance of p 2 in CD95-Ab vs. saline liver samples (n = 5 per group). (F) Venn diagram including the 751 genes upregulated in livers of mice injected with CD95-Ab & the H3K9Ac ChIP-seq data on eight-week-old mouse livers in ENCODE showing a high degree of overlap (Hypergeometric test; p value: 9.643501e−58). (G) Chart generated using custom annotation scripts shows that response to external stimulus including inflammatory & defense response processes, & cytokine-cytokine receptor interaction pathways were enriched among the 467 genes overlapping between the two groups according to KEGG pathways. Means ± SDs are shown; t test; *p 0.05, One‐way ANOVA). ZO‐1 level: P 0.05, One‐way ANOVA). ZO‐1 level: P 1 indicate brighter nuclear staining for NF-kappa B. (c) BV2 cells were incubated with 200 ng/mL LPS in the presence of ENERGI-F704 for 24 h. After treatments, cell lysates were used to determine the levels of NF-kappa B using Western blotting. Data are presented as the mean ± SEM of three independent experiments (one-way ANOVA; * & **, P < 0.05 & P < 0.01; specific comparison to LPS-treated control). Representative images of three independent experiments are shown. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25025067), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-501_mouse-monoclonal-beta-actin-antibody-ac-15-310202416175284.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - Sortilin forms homodimers in the extracellular & intracellular domains with intermolecular disulfide bonds in HEK293 cells.A, schematic of FLAG-sortilin Full, ECD+TMD, & ICD+TMD. SP, signal peptide; PP, propeptide. B & C, protein expression of FLAG-sortilin Full, ECD+TMD, & ICD+TMD was validated in reducing (B) & non-reducing (C) Western blotting using anti-FLAG antibody. FLAG-sortilin Full & ECD+TMD form homodimers & multimers. Empty vector was used as a control. D, HEK293 cells transiently overexpressing FLAG-sortilin Full or ECD+TMD were treated with a cross-linker, BS3, & the cell lysates were used for reducing Western blotting with anti-FLAG antibody, showing dimerization of sortilin Full & ECD+TMD (n = 3). E, HEK293 cells stably overexpressing FLAG-sortilin ICD+TMD (FLAG-sortilin ICD+TMD HEK293 cells) were incubated with DMSO (Control), 20 μmol/liter MG-132 (MG) or 10 μmol/liter chloroquine (Chlo) for 7 h, & then reducing Western blotting was performed using anti-sortilin antibody. MG-132 increased the protein expression of FLAG-sortilin ICD+TMD, but chloroquine did not (n = 3). F, FLAG-sortilin ICD+TMD HEK293 cells were incubated with DMSO or MG-132 (2–20 μmol/liter) for 7 or 24 h. MG-132 increased FLAG-sortilin ICD+TMD in a time- & concentration-dependent manner (n = 3). G, following 16-h incubation of HEK293 cells (Control) or FLAG-sortilin ICD+TMD HEK293 cells (ICD+TMD) with MG-132 (5 μmol/liter) & immunoprecipitation with anti-FLAG antibody, non-reducing Western blotting showed dimerization of sortilin ICD+TMD using anti-sortilin antibody (n = 3). Monomers, homodimers, & multimers are abbreviated as MO, D, & MU, respectively. IB, immunoblotting. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29382723), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-501_mouse-monoclonal-beta-actin-antibody-ac-15-310202416161825.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - RAF1/ERK signalling is preferentially required for PANC1 cell survival in the absence of exogenous insulin. (A) Effects of different small molecule inhibitors on propidium iodide (PI) incorporation (PI) in PANC1 cells were tracked & expressed as the fold change in the percent of PI & Hoechst co-positive cells over total Hoechst positive cells at that hour relative to t =0 hour. Kinetic data were analyzed relative to serum-free control by two-way ANOVA (n =3) Data points that have been shaded solid black represent statistical significance when compared to non-treated conditions at that time point. # Indicates statistical significance in cells treated with Akti1/2 when compared to control at that time point. (B) Average number of PI positive cells over time of each treated group in Figure 5A is shown as a histogram expressed in arbitrary units (AU). GW5074 exhibited statistical significance, where as other treatments did not yield significance. U0126 p = 0.38, GW5074 *p = 0.0005, Akti-1/2 p = 0.395, Wort. p = 0.292 (n = 3). (C) The effect of 24 hours treatment with inhibitors on cleaved caspase 3 protein levels in PANC1 cells. This is a representative immunoblot of three independent biological replicates (n =3). (D-E) PANC1 cells were serum starved & treated with either DMSO, 10 μM GW5074, 10 μM U0126, 200 nM Akti-1/2 & 1 mM wortmannin (wort.) for 24 hours & 120 hours (n =4-5). Cell viability of PANC1 cells was expressed as the fold change of the treated relative to control. (C-E) One-way ANOVA analysis with Bonferroni post-test was performed. *Represents statistical significance of p < 0.05 where treated groups are compared to control (-) in the post-hoc test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25373319), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-501_mouse-monoclonal-beta-actin-antibody-ac-15-310202416175255.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - Analysis of HCAR expression in D2 & D2G retina & ON. a, b Bar graphs showing Hcar1 (a), ***p = 0.0001, & Hcar2 (b) mRNA normalized to Hprt mRNA by qRT-PCR; n = 8 ON per group. c Immunohistochemical analysis of HCAR1 (red) expression in the untreated (Unt) & keto D2 retina & ON. GFAP (green) labels Müller glia & astrocytes, Iba1 (cyan) labels microglia, & DAPI (blue) stains nuclei. Arrows indicate colocalization of HCAR1 with Iba1+ microglia & GFAP+ astrocytes. d, e Percentage of mean fluorescence of HCAR1 in the inner retina (d), **p = 0.0036, & in the ROI of the proximal ON (e), ***p = 0.0001; five retinae per group, with five sections/retina. f Western blot analysis of HCAR1 protein level in retina. g Quantification by densitometry of HCAR1 protein normalized to beta -actin, ***p = 0.0008; n = 3 blots per group, each with independent samples. h HCAR1 protein in the ON normalized to beta -actin levels, as determined by capillary electrophoresis, **p = 0.0025; n = 3 ON per group. All bar graphs are presented as the mean ± SEM, n = 5, analyzed by two-tailed unpaired t test. Scale bar, 20 μm Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30424795), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-501_mouse-monoclonal-beta-actin-antibody-ac-15-31020241616028.jpg)
![Simple Western: beta-Actin Antibody (AC-15) [NB600-501] - iPSC-RPE from an ARB donor show reduced levels of Best1 expression compared to five different iPSC-RPE control lines. (A) To compare Best1 protein expression levels between different iPSC-RPE lines, beta -actin was used as a loading control. (B) While iPSCs displayed no detectable Best1 protein expression, all shown iPSC-RPE lines – regardless of donor origin – displayed detectable Best1 protein expression. (C) The three control iPSC-RPE lines derived from unrelated, unaffected donors all exhibited similar levels of Best1 protein expression. The dad exhibited reduced levels compared to the unrelated controls & the mom showed levels that were about 50% that of the dad. This was expected as the antibody used cannot detect the mutant Best1I366fsX18 which both the mom & the ARB patient are heterozygous for. Best1 expression levels in the ARB iPSC-RPE line were about a quarter of the levels observed in the Mom 214 iPSC-RPE clone. (D) Widefield immunofluorescent staining of Best1 reveals basolateral staining in each of the iPSC-RPE lines, indicating that Best1 protein is properly localized regardless if Best1R141H and/or Best1I366fsX18 are present. Immunofluorescent signal was notably weaker in the ARB iPSC-RPE clones than in the control clones. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-018-21651-z), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-501_mouse-monoclonal-beta-actin-antibody-ac-15-310202416163795.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - Nifedipine & the expression p-AMPK, SREBP-1/2(nuclear), PPAR-alpha (nuclear) & lipin-1 (nuclear) in 48 h. (a) The AMPK/actin was upregulated to 107.1%, 112.6%, & 116.4%, significantly at doses of 7.5, 15, & 30 μM (p < 0.05), the ratio p-AMPK/AMPK was downregulated to 82.1%, 58.7%, & 49.9%, respectively. (b,c) SREBP-1 was activated in control. The SREBP-1/HDAC was upregulated to 109.9% & 132.0% by nifedipine at doses of 7.5 & 30 μM, respectively (p < 0.01); The SREBP-2 were elevated to 127.5%, 146.7% & 161.0% by nifedipine at doses of 7.5, 15 & 30 μM, respectively (p < 0.05 in 7.5 μM, p < 0.01 in 15 & 30 μM) (d) nifedipine downregulated PPAR-alpha . The PPAR alpha /Lamin B was suppressed from 80.2%, 85.6%, to 96.4% compared to control (100%) upon administration of nifedipine at doses 7.5, 15 & 30 μM, respectively. (p < 0.05 in 15 & 30 μM) (e) Lipin-1 was activated in control. The lipin-1/lamin B was upregulated after nifedipine treatment to 102.5%, 115.8% & 121.1%, respectively, by nifedipine at doses of 7.5, 15, & 30 μM, respectively (p < 0.05 in 15 & 30 μM). p-values ≤ 0.05 (marked as *) were considered statistically significant. In addition, p-values ≤ 0.01 are marked as **. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30934807), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-501_mouse-monoclonal-beta-actin-antibody-ac-15-310202416173528.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - JEV NS5 interacts with mitochondrial trifunctional protein (MTP), the enzyme complex involved in LCFA beta -oxidation.(A) Western blot analysis of protein levels of the indicated proteins in A549 cells with JEV infection (MOI = 10) or NS5-Flag overexpression. (B) Western blot analysis of V5-tag, Flag-tag, & actin in HEK293T cells co-transfected with HADH alpha -V5-His plus the indicated plasmids expressing Flag-tagged JEV viral proteins for 24 h, then immunoprecipitated with anti-Flag affinity gel. WCL, whole-cell lysates. (C) Immunoprecipitation (IP) analysis with control IgG or anti-Flag affinity gel in A549, GFP-A549 & NS5-Flag-A549 cells. The protein bands identified as HADH alpha & HADH beta are indicated by arrows. (D) IP with anti-Flag affinity gel & Western blot analysis with the indicated antibodies in HEK293T cells co-transfected with vector control or NS5-Flag plus HADH alpha -V5-His or HADH beta -HA for 24 h. (E) IP analysis with nickel beads & Western blot analysis with the indicated antibodies in HEK293T cells adsorbed with JEV for 3 h, then transfected with vector control, HADH alpha -V5-His or HADH beta -V5-His for 24 h. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.ppat.1004750), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-501_mouse-monoclonal-beta-actin-antibody-ac-15-310202416163768.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - The effect of AM1241, SB203580, & PDTC on the thermal threshold & the expression of P2Y12 & P2Y13 receptors. Data are presented as TWL. All values represent mean ± standard deviation. a Comparison of thermal stimulation pain threshold in the ipsilateral hind paw of rats (n = 8). Spinal ADPbetaS injection reduced TWL from days 3 to 7 after ADPbetaS injection. *P < 0.05 compared w/ control group. Pretreated w/ AM1241 (100 PM, 20 min), SB203580 (50 μM), or PDTC (5 μg/10 μl) significantly inhibited the reduced w/drawal threshold days 3 to 7 in ADPbetaS-treated rats, respectively (compared w/ ADPbetaS-treated rats, AM1241: P < 0.05; SB203580: P < 0.05; PDTC: P < 0.05). b RT-PCR results show the expression of P2Y12 mRNA expression in the dorsal spinal cord of the rats in every groups (n = 8 per group). *P < 0.05 means comparison w/ the control group; +P < 0.05 means comparison w/ the ADPbetaS-treated rats. c RT-PCR results show the expression of P2Y13 mRNA expression in the dorsal spinal cord of the rats in every group (n = 8 per group). *P < 0.05 means comparison w/ the control group; +P < 0.05 means comparison w/ the ADPbetaS-treated rats. d Western blotting image of P2Y12R expression. The top panel the target band, P2Y12R, & the bottom one for the loading control beta-actin. e Western blotting quantitative analysis of the P2Y12R expression in the dorsal spinal cord of the rats. *P < 0.05 means comparison w/ the control; +P < 0.05 means comparison w/ the ADPbetaS-treated rats. f Western blotting quantitative analysis of the P2Y13R expression in the dorsal spinal cord of the rats. *P < 0.05 means comparison w/ the control; +P < 0.05 means comparison w/ the ADPbetaS-treated rats Image collected & cropped by CiteAb from the following publication (//jneuroinflammation.biomedcentral.com/articles/10.1186/s12974-017-0960-0), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-501_mouse-monoclonal-beta-actin-antibody-ac-15-31020241617357.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - Effects of insulin on AKT & ERK phosphorylation & cell viability in primary human pancreatic duct cells. Phosphorylated AKT & ERK were measured in primary pancreatic exocrine cultures treated with the indicated concentrations of insulin for 5 minutes (A, B) & 24 hours (C, D) (n =3-4) Fold refers to the fold change of sample relative to control at the same time point. (E) Quantification of automated cell-counting studies employing live-cell imaging of Hoechst-labeled cell cultures over 60 hours. (n =3). (F) Quantification of proliferation by BrdU staining of treated relative to untreated over 3 days (n =4). (G) Quantification of the average number of dying/dead treated cells, propidium iodide (PI) labeled, over 60 hours relative to non-treated cells. (n =3). (H) Human exocrine cells were exposed to 0, 0.2, 2, 20, 200 nM insulin for 3 days. Bright-field images are representative of 3 cultures. (I) Effects of inhibition of RAF1/ERK signalling on PI incorporation with 10 μM GW5074 or AKT signalling with 100 nM Akti1/2 on human primary pancreatic exocrine cell viability (n =3). SF denotes serum free. Repeated Measures ANOVA analyses with Bonferroni’s post-test were performed. *Represents statistical significance of p < 0.05 when compared to DMSO control. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25373319), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-501_mouse-monoclonal-beta-actin-antibody-ac-15-31020241616087.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - Intrathecal injection of SB203580 (50 μM) or PDTC (5 μg/10 ml) suppressed the increased expression of P2Y12 & P2Y13R in the dorsal spinal cord of CCI rats. a Comparison of thermal stimulation pain threshold in the ipsilateral hind paw of the rats (n = 8). Data are presented as TWL. CCI reduced TWL from days 1 to 7 after nerve injury. *P < 0.05 compared with control group. Pretreated with SB203580 (50 μM) or PDTC (5 μg/10 ml) significantly inhibited the reduced withdrawal threshold days 1 to 7 in CCI rats, respectively (compared with vehicle-treated CCI group, SB203580: +P < 0.05; PDTC: +P < 0.05). b RT-PCR results show the expression of P2Y12 mRNA expression in the rat dorsal spinal cord (n = 8 per group). *P < 0.05 means comparison with the control group; +P < 0.05 means comparison with the vehicle-treated CCI group. c RT-PCR results show the expression of P2Y13 mRNA expression in the rat dorsal spinal cord (n = 8 per group). *P < 0.05 means comparison with the control group; +P < 0.05 means comparison with the vehicle-treated CCI group. d Western blotting image of P2Y12R & P2Y13R expression. The top panel was the target band, & the bottom one was for the loading control beta-actin. e Western blotting quantitative analysis of the P2Y12R expression in the rat dorsal spinal cord. *P < 0.05 means comparison with the sham group; +P < 0.05 means comparison with the vehicle-treated CCI group. f Western blotting quantitative analysis of the P2Y13R expression in the rat dorsal spinal cord. *P < 0.05 means comparison with the sham group; +P < 0.05 means comparison with the vehicle-treated CCI group Image collected & cropped by CiteAb from the following publication (//jneuroinflammation.biomedcentral.com/articles/10.1186/s12974-017-0960-0), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-501_mouse-monoclonal-beta-actin-antibody-ac-15-310202416173522.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - Effects of HSM on the expression of P2X4R & P2X7R & ROS production in human macrophages.Cells were pretreated with various concentrations (1 or 2%) of HSM extract for 20 h, followed by treatment with LPS (0.5 μg/ml) for 3 h & ATP (5 mM) for 1 h. (a) The mRNA expression levels of P2X4R & P2X7R were determined by RT-PCR, using beta -actin as the internal control. (b) P2X4R & P2X7R mRNAs were quantified using real-time PCR. beta -actin gene expression was used for normalization. The results are expressed as fold changes, considering one as the value of untreated cells. (c) Cell lysates were analyzed by Western blot analysis used specific anti-P2X4R & anti-P2X7R antibodies. (d) ROS production was measured with the total ROS detection kit, using a fluorescence microplate reader. Pyocyanin (200 μM), a ROS inducer, was used as a positive control for ROS formation. Data are presented as means ± SE of three experiments preformed in duplicate. #P < 0.01 versus untreated cells. versus HSM-untreated control (ethanol) cells. *P < 0.01 versus HSM-untreated control (ethanol) cells. †P < 0.05 versus HSM (1%) treated cells. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23459183), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-501_mouse-monoclonal-beta-actin-antibody-ac-15-310202416161830.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - Zinc-finger motifs of ZAP are required for JEV RNA binding & its antiviral activity.(A) Schematic representation of human ZAP isoforms (ZAP-L, 902 a.a. & ZAP-S, 699 a.a.). The four tandem CCCH-type zinc-finger (ZF) motifs within the N-terminus of ZAP are shown as solid black boxes. Deletion of the four ZFs (a.a. 73–193) are indicated with a dashed line. (B) 293T/17 cells infected with JEV (MOI = 5) for 16 h were transfected with plasmids expressing EGFP, WT or ZF-deleted ZAP-L-V5 & ZAP-S-V5 for additional 24 h. The viral RNA bound with V5-tagged proteins was pulled down by anti-V5 agarose affinity gel & amplified by RT-PCR with JEV 3′-UTR specific primers (middle panel). RT-PCR of input viral RNA in JEV-infected cells (lower panel). Western blot analysis of the immunoprecipitated ZAP-L & ZAP-S (WT & del4ZFs) (upper panel). (C-E) The indicated cells were infected with JEV (MOI = 5) for 10 h. Cell lysates, total RNA, & culture supernatants were determined for the indicated proteins by western blot (C), viral RNA by RT-PCR (D), & viral titer by plaque assay (E). Representative data from three independent experiments shown as mean ± SD (n = 3) were analyzed by two-tailed Student’s t test. *** P≤0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30016363), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-501_mouse-monoclonal-beta-actin-antibody-ac-15-310202416175223.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - Effects of HSM on IL-1 beta gene expression & secretion in human macrophages.Cells were pre-treated with either 1 or 2% of HSM extract for 20 h, followed by treatment with LPS (0.5 μg/ml) for 3 h & with ATP (5 mM) for 1 h. (a) The mRNA expression levels of IL-1 beta were determined by RT-PCR analysis. (b) IL-1 beta mRNAs were quantified using real-time PCR. beta -actin gene expression was used for normalization. The results are expressed as fold changes, considering one as the value of untreated cells. (c) The amount of IL-1 beta in cell culture supernatants was detected by ELISA. (d) The presence of IL-1 beta in cell lysates & cell culture supernatants were analyzed by Western blot analysis. Data are presented as means ± SE of three experiments performed in duplicate. #P < 0.01 versus untreated cells. *P < 0.01 versus HSM-untreated (ethanol-treated) control cells. †P < 0.05 versus HSM (1%) treated cells. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23459183), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-501_mouse-monoclonal-beta-actin-antibody-ac-15-31020241616012.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - Intrathecal injection of AM1241 (100pM) attenuated CCI-induced hyperalgesia & increased expression of p-p38MAPK & NF-kappaBp65 in the rat dorsal spinal cord (n = 8 per group). a Western blotting image of p-p38MAPK expression. The top panel was the target band, p-p38MAPK, & the bottom one was for the loading control beta-actin. b Western blotting quantitative analysis of the p-p38MAPK expression in the rat dorsal spinal cord. *P < 0.05 means comparison with the sham group; +P < 0.05 means comparison with the vehicle-treated CCI group. c Western blotting image of NF-kappaBp65 expression. The top panel was the target band, NF-kappaBp65, & the bottom one was for the loading control beta-actin. d Western blotting quantitative analysis of the NF-kappaBp65 expression in the dorsal spinal cord of the rats. *P < 0.05 means comparison with the sham group; +P < 0.05 means comparison with the vehicle-treated CCI group Image collected & cropped by CiteAb from the following publication (//jneuroinflammation.biomedcentral.com/articles/10.1186/s12974-017-0960-0), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-501_mouse-monoclonal-beta-actin-antibody-ac-15-31020241616015.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - Intralipid enhances the cytotoxicity of Abraxane in tumors. (A) The box-and-whisker plot represents the amount of paclitaxel in tumors determined by LC/MS. The number above the box denotes the median amount of remaining paclitaxel in the tumor tissues. (B) Western blot analysis of the apoptosis signal, cleaved caspase-3, in the tumors at 24 & 48 hrs after Abraxane treatment. beta -actin served as a loading control. The blots of caspase-3 & beta -actin are cropped from different parts of the same gel. The intensity of each band of the cleaved caspase-3 was measured by ImageJ software (NIH) & normalized to its own signal of beta -actin. The values summarized in the box-and-whisker plot denote the relative intensities compared with those in the control group. (C,D) The immunohistochemistry of cleaved caspase-3 (C) & the TUNEL assay (D) are analyzed in 48 hrs tumor sections. Original: 200x magnification; Inserts; 400x magnification. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32071352), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-501_mouse-monoclonal-beta-actin-antibody-ac-15-310202416163737.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - The effect of minocycline on the expression of P2Y12 & P2Y13 receptors. All values represent mean ± standard deviation. a RT-PCR results show the expression of P2Y12 mRNA expression in the rat dorsal spinal cord (n = 8 per group). *P < 0.05 means comparison with the sham group; +P < 0.05 means comparison with the CCI rats. b RT-PCR results show the expression of P2Y13 mRNA expression in the rat dorsal spinal cord (n = 8 per group). *P < 0.05 means comparison with the sham group; +P < 0.05 means comparison with the CCI rats. c Western blotting quantitative analysis of the P2Y12R expression in the rat dorsal spinal cord. *P < 0.05 means comparison with the control; +P < 0.05 means comparison with the ADPbetaS-treated rats. d Western blotting quantitative analysis of the P2Y13R expression in the rat dorsal spinal cord. *P < 0.05 means comparison with the control; +P < 0.05 means comparison with the ADPbetaS-treated rats. e Western blotting image of P2Y12R expression. The top panel was the target band, P2Y12R, & the bottom one was for the loading control beta-actin. f Western blotting image of P2Y13R expression. The top panel was the target band, P2Y13R, & the bottom one was for the loading control beta-actin Image collected & cropped by CiteAb from the following publication (//jneuroinflammation.biomedcentral.com/articles/10.1186/s12974-017-0960-0), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-501_mouse-monoclonal-beta-actin-antibody-ac-15-31020241616081.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - Effects of HSM on inflammasome components & caspase-4 activation in human macrophages.Cells were pretreated with various concentrations (1 or 2%) of HSM extract for 20 h, followed by treatment with LPS (0.5 μg/ml) for 3 h & ATP (5 mM) for 1 h. (a) The mRNA expression levels of ASC, NLRP1, NLRP3 & caspase-4 were determined by RT-PCR, using beta -actin as the internal control. (b) ASC, NLRP1, NLRP3 & caspase-4 mRNAs were quantified using real-time PCR. beta -actin gene expression was used for normalization. The results are expressed as fold changes, considering one as the value of untreated cells. (c) Cell lysates were analyzed by Western blot analysis using specific anti-ASC, anti-NLRP1 & anti-NLRP3 antibodies. (d) Cell lysates were analyzed for protein levels of caspase-4 by Western blot analysis. beta -actin was used as an internal control. Data are presented as means ± SE of three experiments preformed in duplicate. #P < 0.01 versus untreated cells. versus HSM-untreated control (ethanol) cells. *P < 0.01 versus HSM-untreated control (ethanol) cells. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23459183), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-501_mouse-monoclonal-beta-actin-antibody-ac-15-31020241617147.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - The cleaved MFN fragments were further degraded by host proteasome machinery.(A) Western blot analysis of A549+on/MFN1 (lane 1–6) & /MFN2 (lane 7–12) cells with Dox treatment (all lanes) & DENV infection (lane 3–6 & 9–12). The cells were infected with DENV serotype 2 (moi 5) for 24 h, then incubated in culture media containing Dox (1 μg/ml) with (lanes 5–6 & 11–12) or without MG132 (0.5 μM) for 16 h. (B) Western blot analysis of four different serotypes DENV-infected A549 cells incubated with MG132-containing medium. (C) Western blot analysis of endogenous MFN1 & 2 cleavage in A549 stable cells overexpressing WT or protease-dead mutant (S135A) of DENV NS2B3 with or without 18-h treatment with MG132 (0.5 μM). Filled arrow: full-length; open arrow: cleaved product; star: non-specific band. The longer exposure images for endogenous MFN1 & 2 signals are also shown in panels B & C. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.ppat.1005350), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-501_mouse-monoclonal-beta-actin-antibody-ac-15-310202416175283.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - ENERGI-F704 decreases LPS-induced NO, iNOS, COX-2, & PGE2 production in BV2 cells. BV2 cells were stimulated with 200 ng/mL LPS & subsequently treated with either ENERGI-F704 or AICAR for 24 h. (a) Levels of NO in the culture of BV2 cell were determined. (b) After treatments, cell lysates were used to determine the level of iNOS & COX-2 using Western blotting. (c) LPS-treated BV2 cells were treated with ENERGI-F704 in cotreatment with or without compound C for 24 h. Cell lysates were used to determine the level of iNOS & COX-2 using Western blotting. (d) LPS-induced BV2 cells were treated with ENERGI-F704 in cotreatment with or without compound C for 48 h, & the level of PGE2 in the culture medium was determined. Data are presented as the mean ± SEM of three independent experiments (two-way ANOVA; *, **, & ***, P < 0.05, P < 0.01, & P < 0.01; specific comparison to LPS-treated control). Representative images of three independent experiments are shown. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25025067), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-501_mouse-monoclonal-beta-actin-antibody-ac-15-310202416154616.jpg)
![Simple Western: beta-Actin Antibody (AC-15) [NB600-501] - iPSC-RPE from all donors express RPE marker proteins. (A) As a loading control, each iPSC-RPE line (ARB patient, the patient’s parents, & three unrelated, unaffected controls) as well as iPSCs (negative control) were blotted for beta -actin. (B) Unlike iPSCs, all iPSC-RPE lines showed robust expression of CRALBP. (C) Just like CRALBP, iPSC-RPE from the patient, the patient’s mom, the patient’s dad, & the three unrelated, unaffected controls all expressed RPE65. The negative control (iPSCs) had no detectable RPE65 protein expression. (D) Each of the iPSC-RPE lines but not iPSCs displayed strong expression of the RPE marker Mer-tk. (E) The relative expression levels for each of these three markers is summarized for iPSCs & all of the iPSC-RPE lines. Graphs show the summary of expression for each marker from three separate blotting experiments. Variability between each of the controls as well as between the different iPSC-RPE lines was observed for each of the RPE markers. Control 4 displayed the highest levels of CRALBP, Control 138 had the highest levels of RPE65, & Control 1 showed the highest levels of Mer-tk. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-018-21651-z), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-501_mouse-monoclonal-beta-actin-antibody-ac-15-31020241616032.jpg)
![Western Blot: beta-Actin Antibody (AC-15) [NB600-501] - Effects of MFN1 or MFN2 overexpression on DENV infection.(A) Western blot analysis of A549+on/HA-MFN1 cells induced with Dox (1 μg/ml) or not for 18 h, then infected with DENV serotype 2 for 24 or 48 h by the indicated moi. The relative ratios of band intensity were quantified by ImageJ. p.i. (h): hours post infection. (B) DENV plaque-forming assay of culture supernatants from A549+on/HA-MFN1 cells cultured with or without Dox (1 μg/ml) for 18 h, then infected with DENV (moi 0.1 or 10) as indicated. Data in panels B-D & F-G are mean ± SD (n = 3 per group) & were compared by two-tailed Student’s t test. (C) RT-qPCR analysis of IFN beta mRNA expression at indicated time point in DENV-infected (moi 10) A549+on/HA-MFN1 cells with or without an 18 h-Dox-pretreatment. (D) Analysis of antiviral activity against dSinF-Luc/2A virus in culture media from A549+on/HA-MFN1 cells with DENV infection (moi 5, 48 h) with or without 18-h Dox pretreatment. (E) Western blot analysis of A549+on/HA-MFN2 cells induced with Dox (1 μg/ml, 18 h) or not, then infected with DENV (moi 10) for the indicated time. (F & G) Analysis of the culture supernatants derived from panel E for DENV titer (F) & LDH release (G). (H) Flow cytometry of A549+on/HA-MFN2 cells double stained with JC-1 & annexin V. Cells were infected with DENV (moi 5) for 48 h with or without 18-h Dox pre-treatment. Decreased red/green fluorescence ratio of JC-1 represents disrupted MMP. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.ppat.1005350), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-501_mouse-monoclonal-beta-actin-antibody-ac-15-31020241618263.jpg)
![Immunohistochemistry-Paraffin: Goat Polyclonal AIF-1/Iba1 Antibody [NB100-1028] - AIF-1/Iba1 immunoreactivity in an FFPE section of mouse spleen. NB100-1028 was diluted to 1ug per mL and was left on tissue sections for 30m at room temperature. Secondary was horse anti goat HRP polymer. Image from a verified customer review.](http://images.novusbio.com/fullsize/antibody/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-immunohistochemistry-paraffin-752024135211..jpg)
![Immunohistochemistry-Paraffin: Goat Polyclonal AIF-1/Iba1 Antibody [NB100-1028] - AIF-1/Iba1 immunoreactivity in an FFPE section of human tonsil. NB100-1028 was diluted to 1ug per mL and was left on tissue sections for 30m at room temperature. Secondary was horse anti goat HRP polymer. Image from a verified customer review.](http://images.novusbio.com/fullsize/antibody/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-immunohistochemistry-paraffin-7520241463..png)
![Immunohistochemistry-Paraffin: Goat Polyclonal AIF-1/Iba1 Antibody [NB100-1028] - AIF-1/Iba1 immunoreactivity in an FFPE section of equine spleen. NB100-1028 was diluted to 1ug per mL and was left on tissue sections for 30m at room temperature. Secondary was equine anti goat HRP polymer. Image from a verified customer review.](http://images.novusbio.com/fullsize/antibody/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-immunohistochemistry-paraffin-2852024102248..png)
![Immunocytochemistry/ Immunofluorescence: AIF-1/Iba1 Antibody [NB100-1028] - Microglia proliferate in non‐APP mice upon peripheral immune challengeA, BIba‐1, Ki67, & DAPI staining in the cortex & hippocampus of wild‐type & Nlrp3−/− (5 & 15 months old). Microglia proliferate upon LPS injection (white arrows). Non‐microglia cells proliferation was observed as well (yellow arrows). Scale bar: 20 μm.CQuantification of microglial proliferation in cortex (left panel) & hippocampus (right panel) (mean of 5 ± SEM; two‐way ANOVA followed by Tukey's post hoc test, *P 1.5, FDR-corrected p1.5, FDR-corrected p<0.05) to identify GO terms, including inflammatory response (b). The volcano plot shows significant DEGs derived from the NanoString analysis of the brains of Plcg2 inactivation (PLCG2 inact, n=3) & WT (n=3) mice (1-month male) (c). Immunostaining of microglial markers with IBA1 (green) & P2RY12 (red) & quantification of percent area in brain sections of 1-month-old male WT & PLCG2 inact demonstrate unchanged microglial morphology & area coverage (d). GO gene ontology, BP biological process, DEGs differentially expressed genes, FDR false discovery rate Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35180881), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415483623.jpg)
![Immunocytochemistry/ Immunofluorescence: AIF-1/Iba1 Antibody [NB100-1028] - Representative & quantitative immunohistochemistry of the peri-infarct cortex before the bregma (coordinate + 0.58) in normal WT, normal sEH KO, MCAO WT, MCAO sEH KO, MCAO with vehicle treatment & MCAO with AUDA treatment mice (n = 2 for normal groups, n = 5–6 for all groups subjected to MCAO). (A–F, S) The number of CD31-positive endothelial cells significantly increased in the sEH KO before & after MCAO & post-MCAO AUDA-treated mice, while (G–L) Note the increased phosphorylated TrkB (p-TrkB) immunoreactivity that partially co-localized with NeuN-positive neurons, particularly in the sEH KO & AUDA-treated mice (arrows) (T). The percentage of NeuN- & p-TrkB-positive double labeling in the neuronal population was significantly increased compared to that in the corresponding controls. (M–R, U–V) GFAP-positive astrogliosis & Iba1-positive microglial infiltration decreased in post-MCAO sEH KO & AUDA treatment groups relative to that in the corresponding controls. The scale bar represents 50 µm. *p < 0.05, **p < 0.01, ***p < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29311641), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415482273.jpg)
![Immunocytochemistry/ Immunofluorescence: AIF-1/Iba1 Antibody [NB100-1028] - Representative & quantitative immunohistochemistry of the peri-infarct cortex before the bregma (coordinate + 0.58) in normal WT, normal sEH KO, MCAO WT, MCAO sEH KO, MCAO with vehicle treatment & MCAO with AUDA treatment mice (n = 2 for normal groups, n = 5–6 for all groups subjected to MCAO). (A–F, S) The number of CD31-positive endothelial cells significantly increased in the sEH KO before & after MCAO & post-MCAO AUDA-treated mice, while (G–L) Note the increased phosphorylated TrkB (p-TrkB) immunoreactivity that partially co-localized with NeuN-positive neurons, particularly in the sEH KO & AUDA-treated mice (arrows) (T). The percentage of NeuN- & p-TrkB-positive double labeling in the neuronal population was significantly increased compared to that in the corresponding controls. (M–R, U–V) GFAP-positive astrogliosis & Iba1-positive microglial infiltration decreased in post-MCAO sEH KO & AUDA treatment groups relative to that in the corresponding controls. The scale bar represents 50 µm. *p < 0.05, **p < 0.01, ***p < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29311641), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415483641.jpg)
![Immunocytochemistry/ Immunofluorescence: AIF-1/Iba1 Antibody [NB100-1028] - Norgestrel reduces pro-inflammatory & promotes anti-inflammatory phenotypes in rd10 microglia.(A) RT-qPCR analysis detected similar levels of mRNAs encoding progesterone receptor membrane complexes 1 & 2 (PGRMC1, PGRMC2) & all three membrane progesterone receptor isoforms, alpha , beta & gamma (mPR alpha , mPR beta , mPR gamma ) in rd10 retinal microglial cells. Classical progesterone receptor (PR A/B) was not expressed. Actin, HPRT & GAPDH served as reference genes. (B) Immunolabeling confirmed the presence of these progesterone receptors in primary rd10 microglial cells. Hoechst (blue) staining reveals the cell nuclei. Scale bar represents 10μm. (C) Fluorescent microscopic images of primary rd10 microglia immunolabeled for (C) (i) markers of activation (CD68) & pro-inflammation (M1) (iNOS) & (C) (ii) anti-inflammatory activation (M2) (MRC1); after treatment with 20 μM Norgestrel over 24h. Norgestrel reduced pro-inflammatory & increased anti-inflammatory markers in rd10 microglia. Scale bar 10μm. (D) Quantification of fluorescence intensity of (D) (i) CD68 & iNOS & (D) (ii) MRC1 in primary rd10 microglial cultures following Norgestrel treatment over 24h. N = 8 mice, n = 4 technical replicates per group. (E) Nitrite concentration in the media of rd10 microglia in vitro treated with Norgestrel or vehicle over 24hr. Norgestrel significantly reduced nitrite release from rd10 microglia. N = 8 biological replicates, n = 2 technical replicates per sample. Results are presented as mean ± SEM (t-test, *p<0.05, ***p<0.005, ****p<0.001). Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0165197), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415482243.jpg)
![Immunohistochemistry: AIF-1/Iba1 Antibody [NB100-1028] - Temporal activation of caspase-8 in Iba1-positive myeloid cells. Frozen tissue sections from mice upon pMCAO (n = 9) were analyzed by immunohistochemistry for expression of active caspase-8 or for expression of the microglia/macrophage marker Iba1. The contralateral side to the ischemic area was used an internal control for each animal. A small increase in body size of Iba1 positive cells was detected in the peri-infarct area at 6 h, with larger increase in cell body & numbers of cells expressing Iba1 detected at 24 & 48 h post occlusion (a). Cleaved caspase-8 was detected at low levels at 6 h, but a significant increase in expression levels was observed at 24 & 48 h in the peri-infarct area, but not at the contralateral side (a). Double immunofluorescent staining revealed that increased active caspase-8 expression was localized in Iba1-positive cells (b). Scale bar represent 100 μm in IHC images (a) & 10 μm in IF images (b) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27566702), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-31020241548514.jpg)
![Western Blot: AIF-1/Iba1 Antibody [NB100-1028] - GM1 effects on brain microglia in vivo, after peripheral administration of LPS. A Schematic representation of in vivo administration of GM1 after LPS-induced systemic inflammation in mice (N = 5 per treatment). B Representative images of Iba-1 stained microglia in the cortex of control animals infused with vehicle (CTRL) or GM1 (CTRL + GM1), & in animals treated with LPS & subsequently infused with vehicle artificial cerebrospinal fluid (LPS) or GM1 (LPS + GM1). C Immunoblot in whole brain lysates & densitometric analysis show LPS-dependent increase in Iba 1 expression. D Cortical & striatal microglia (Iba-1+ cells) cell body area quantified with MetaXpress software. GM1 administration significantly decreases cell body area in the cortex, but not in the striatum. E IL-6 protein levels in whole mouse brain homogenate. aCSF, artificial cerebrospinal fluid. Bars show mean values ± STDEV. Two-way ANOVA with Tukey’s multiple comparisons test; *p < 0.05, **p < 0.01, ***p < 0.001 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/34991625), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415485114.jpg)
![Immunocytochemistry/ Immunofluorescence: AIF-1/Iba1 Antibody [NB100-1028] - ABIN1 knockdown increases proinflammatory cytokine production & microglial activation. (a-b) Levels of the ABIN1 mRNA & protein were detected 24 h after reperfusion using RT-qPCR & western blot, respectively, to confirm the efficiency of ABIN1 gene knockdown (n = 5 rats per group). (c) ELISA was used to detect the concentrations of TNF-alpha , IL-1 beta & MCP-1 in the peri-infarct cortex at 24 h after reperfusion (n = 5 rats per group). (d) Microglial morphology was observed using immunofluorescence staining for Iba-1 (green) in the peri-infarct cortex at 24 h after reperfusion (n = 3 rats per group). Scale bar = 50 μm. (e & f) Quantification of microglia process endpoints & cell & process lengths/cell (∗∗P < 0.01 compared to the sham group; ##P < 0.01 compared to the MCAO/R group). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33110436), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415485133.jpg)
![Immunocytochemistry/ Immunofluorescence: AIF-1/Iba1 Antibody [NB100-1028] - SCF+G-CSF treatment increases TREM2 expression in the Iba1+ microglia/macrophages surrounding the 6E10+ senile plaques. (A) Representative confocal images of TREM2 (red), 6E10 (purple) & Iba1 (green) triple immunofluorescence staining in the brains of aged APP/PS1 mice. Blue: Nuclear counterstaining by DAPI. (B) Representative orthographic view of z-stack images (12 z-stacks with 1μm intervals) illustrates the location & interaction of TREM2 + cells (red) & 6E10+ A beta plaques (white) in the brains of aged APP/PS1 mice. (C) Quantification data show the percentage of TREM2+ area surrounding the 6E10+ A beta plaques (within 10μm from the border of the A beta plaques) in the brains of aged APP/PS1 mice with or without SCF+G-CSF treatment. (D) Representative orthographic view of z-stack images (12 z-stacks with 1μm intervals) displays the location & interaction of TREM2+/Iba1+ co-expressing cells (yellow) & 6E10+ A beta plaques (white) in the brains of APP/PS1 mice. (E) Quantification data show the percentage of TREM2+/Iba1+ co-expression area in the total of Iba1+ area in the vicinity of 6E10+ A beta plaques in the brains of aged APP/PS1 mice with or without SCF+G-CSF treatment. N=4-5. Mean ± SEM. * p<0.05 by Student’s t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33269098), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415482219.jpg)
![Immunocytochemistry/ Immunofluorescence: AIF-1/Iba1 Antibody [NB100-1028] - SCF+G-CSF treatment increases the association of Iba1+ microglia/macrophages with senile plaques & enhances uptake of 4G8+ A beta by the Iba1+ microglia/macrophages in the brains of aged APP/PS1 mice. (A) Representative confocal images illustrate the association of Iba1+ cells (green) with 4G8+ A beta plaques (red) in the brains of aged APP/PS1 mice. Blue: Nuclear counterstaining by DAPI. (B) Quantification of the percentage of Iba1+ area in/surrounding the 4G8+ A beta plaques in the brains of aged APP/PS1 mice with or without SCF+G-CSF treatment. (C) Representative 3-dimensional projected images reveal the overlapped (yellow) Iba1+ cells (green) with 4G8+ A beta (red) in the brains of aged APP/PS1 mice. The white arrows indicate the co-expression (yellow) of 4G8+ A beta & Iba1+ cells in the brains of aged APP/PS1 mice. (D & E) Representative orthographic view of z-stack images (12 z-stacks with 1μm intervals) shows the co-expression (yellow) of 4G8+ A beta (red) & Iba1+ cells (green) in the brains of aged APP/PS1 mice. (F) Quantification data present the percentage of 4G8+ A beta volume within the Iba1+ cells in the brains of aged APP/PS1 mice treated with or without SCF+G-CSF. N=4-5. Mean ± SEM. *p<0.05 by Student’s t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33269098), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415485142.jpg)
![Immunocytochemistry/ Immunofluorescence: AIF-1/Iba1 Antibody [NB100-1028] - Representative & quantitative immunohistochemistry of the peri-infarct cortex before the bregma (coordinate + 0.58) in normal WT, normal sEH KO, MCAO WT, MCAO sEH KO, MCAO with vehicle treatment & MCAO with AUDA treatment mice (n = 2 for normal groups, n = 5–6 for all groups subjected to MCAO). (A–F, S) The number of CD31-positive endothelial cells significantly increased in the sEH KO before & after MCAO & post-MCAO AUDA-treated mice, while (G–L) Note the increased phosphorylated TrkB (p-TrkB) immunoreactivity that partially co-localized with NeuN-positive neurons, particularly in the sEH KO & AUDA-treated mice (arrows) (T). The percentage of NeuN- & p-TrkB-positive double labeling in the neuronal population was significantly increased compared to that in the corresponding controls. (M–R, U–V) GFAP-positive astrogliosis & Iba1-positive microglial infiltration decreased in post-MCAO sEH KO & AUDA treatment groups relative to that in the corresponding controls. The scale bar represents 50 µm. *p < 0.05, **p < 0.01, ***p < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29311641), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415485140.jpg)
![Immunocytochemistry/ Immunofluorescence: AIF-1/Iba1 Antibody [NB100-1028] - Antibody-mediated Nogo-A blockade decreases the number of cells expressing TNF alpha without affecting the number of Iba1-positive monocytes.Cells expressing TNF alpha , Iba1, & CD68 were labeled on cryosections by immunofluorescence in 4 mouse retinae, 24 h after control IgG or 11C7 injection. a Retinal sections showed many TNF alpha -containing cells located in the inner retina, between the outer plexiform layer & the ganglion cell layer 1 day after control IgG injection. A majority of cells was positive for Iba1 & exhibited vesicular staining of the lysosomal protein CD68, indicating their active state. b The injection of 11C7 strongly attenuated TNF alpha & CD68 expression & to a lower extent the intensity of Iba1 in macrophages/microglia. c Quantification of the number of cells expressing TNF alpha & Iba1 suggesting potent & specific effects of 11C7 on TNF alpha cytokine reduction. Six sections were examined for each retina. Statistics: one-way ANOVA, Dunnett’s post hoc test, **P < 0.01; ****P < 0.0001. Scale bars = 50 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32029703), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415485131.jpg)
![Immunocytochemistry/ Immunofluorescence: AIF-1/Iba1 Antibody [NB100-1028] - SCF+G-CSF treatment increases TREM2 expression in the Iba1+ microglia/macrophages surrounding the 6E10+ senile plaques. (A) Representative confocal images of TREM2 (red), 6E10 (purple) & Iba1 (green) triple immunofluorescence staining in the brains of aged APP/PS1 mice. Blue: Nuclear counterstaining by DAPI. (B) Representative orthographic view of z-stack images (12 z-stacks with 1μm intervals) illustrates the location & interaction of TREM2 + cells (red) & 6E10+ A beta plaques (white) in the brains of aged APP/PS1 mice. (C) Quantification data show the percentage of TREM2+ area surrounding the 6E10+ A beta plaques (within 10μm from the border of the A beta plaques) in the brains of aged APP/PS1 mice with or without SCF+G-CSF treatment. (D) Representative orthographic view of z-stack images (12 z-stacks with 1μm intervals) displays the location & interaction of TREM2+/Iba1+ co-expressing cells (yellow) & 6E10+ A beta plaques (white) in the brains of APP/PS1 mice. (E) Quantification data show the percentage of TREM2+/Iba1+ co-expression area in the total of Iba1+ area in the vicinity of 6E10+ A beta plaques in the brains of aged APP/PS1 mice with or without SCF+G-CSF treatment. N=4-5. Mean ± SEM. * p<0.05 by Student’s t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33269098), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415482237.jpg)
![Immunocytochemistry/ Immunofluorescence: AIF-1/Iba1 Antibody [NB100-1028] - Representative & quantitative immunohistochemistry of the peri-infarct cortex before the bregma (coordinate + 0.58) in normal WT, normal sEH KO, MCAO WT, MCAO sEH KO, MCAO with vehicle treatment & MCAO with AUDA treatment mice (n = 2 for normal groups, n = 5–6 for all groups subjected to MCAO). (A–F, S) The number of CD31-positive endothelial cells significantly increased in the sEH KO before & after MCAO & post-MCAO AUDA-treated mice, while (G–L) Note the increased phosphorylated TrkB (p-TrkB) immunoreactivity that partially co-localized with NeuN-positive neurons, particularly in the sEH KO & AUDA-treated mice (arrows) (T). The percentage of NeuN- & p-TrkB-positive double labeling in the neuronal population was significantly increased compared to that in the corresponding controls. (M–R, U–V) GFAP-positive astrogliosis & Iba1-positive microglial infiltration decreased in post-MCAO sEH KO & AUDA treatment groups relative to that in the corresponding controls. The scale bar represents 50 µm. *p < 0.05, **p < 0.01, ***p < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29311641), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415482285.jpg)
![Immunocytochemistry/ Immunofluorescence: AIF-1/Iba1 Antibody [NB100-1028] - Representative & quantitative immunohistochemistry of the peri-infarct cortex before the bregma (coordinate + 0.58) in normal WT, normal sEH KO, MCAO WT, MCAO sEH KO, MCAO with vehicle treatment & MCAO with AUDA treatment mice (n = 2 for normal groups, n = 5–6 for all groups subjected to MCAO). (A–F, S) The number of CD31-positive endothelial cells significantly increased in the sEH KO before & after MCAO & post-MCAO AUDA-treated mice, while (G–L) Note the increased phosphorylated TrkB (p-TrkB) immunoreactivity that partially co-localized with NeuN-positive neurons, particularly in the sEH KO & AUDA-treated mice (arrows) (T). The percentage of NeuN- & p-TrkB-positive double labeling in the neuronal population was significantly increased compared to that in the corresponding controls. (M–R, U–V) GFAP-positive astrogliosis & Iba1-positive microglial infiltration decreased in post-MCAO sEH KO & AUDA treatment groups relative to that in the corresponding controls. The scale bar represents 50 µm. *p < 0.05, **p < 0.01, ***p < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29311641), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415482247.jpg)
![Immunocytochemistry/ Immunofluorescence: AIF-1/Iba1 Antibody [NB100-1028] - The presence or absence of TRPV1 influences microglial pathophysiological changes in recurrent febrile seizures mice. (A) Images of the cortex immunostained for the microglial marker Iba-1 (visualized in green FITC) & the lysosomal marker CD68/ED1 (visualized in red Alexa Fluor 594) & DAPI (visualized in blue) 5 days after rFS from wild type (WT) & TRPV1−/− mice (Scale bars: 50 μm). (B,C) Bar graph of quantification of Iba1+(B) & Iba1+ ED1+(C) in 5 days after rFS mice cortex. (D) Representative photomicrographs of different microglial morphological subtypes including resting/ramified (Ram), hypertrophic/intermediate (Inter) & round/ameboid (Amoeboid; Scale bars: 5 μm). (E) Quantification of relative percentage of microglia with different morphologies in the cortex of WT & TRPV1−/− mice (n = 6 per groups, **p < 0.01, ***p < 0.001, two-way ANOVA followed by Tukey’s multiple comparisons). (F–H) Representative Immunoblot bands (F) & densitometric analysis of Iba1 expression (G) & ED1 expression (H) were significantly increased in rFS from WT mice than in TRPV1−/− mice. Data were presented as means ± SEM, n = 6 per groups, *p < 0.05, **p < 0.01, ***p < 0.001, two-way ANOVA followed by Tukey’s multiple comparisons. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31680864), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415482254.jpg)
![Immunohistochemistry-Frozen: Goat Polyclonal AIF-1/Iba1 Antibody [NB100-1028] - AD Mouse Model. FxFr:10 µm thickness 1:200. Secondary antibody AF647. Image from a verified customer review.](http://images.novusbio.com/fullsize/antibody/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-immunohistochemistry-frozen-4122024105512..jpg)
![Immunohistochemistry: Goat Polyclonal AIF-1/Iba1 Antibody [NB100-1028] - Pax5 and Iba1 immunoreactivity in a formalin fixed paraffin embedded classic Hodgkin's lymphoma biopsy. Formalin fixed paraffin embedded sections were deparaffinized and rehydrated. Sections then underwent heat induced epitope retrieval in a citrate-based solution for 20min in a food steamer. Sections were cooled, then blocked in phosphate buffered saline containing 0.2% Triton-X100 and 10% normal donkey serum for 1h at room temperature. Sections were then incubated with the primary antibody for 16h at room temperature. The following day slides were washed three times with PBS containing 0.05% Tween-20. Sections were then incubated with donkey anti-goat (647 conjugate) at 5ug per mL for 45min at room temperature. Slides were then washed as above and mounted with a coverslip. Image from a verified customer review.](http://images.novusbio.com/fullsize/antibody/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-immunohistochemistry-332025111028..jpg)
![Analysis of LC3B in HeLa cells using anti-LC3B antibody (red) [Catalog # NB600-1384]. Nuclei were counterstained with DAPI (blue).](http://images.novusbio.com/fullsize/LC3B-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB600-1384-img0033.jpg)
![Analysis of LC3B in treated U87-MG (human glioblastoma astrocytoma) lysates using anti- [Catalog # NB600-1384].](http://images.novusbio.com/fullsize/LC3B-Antibody---BSA-Free-Western-Blot-NB600-1384-img0027.jpg)
![Staining of treated U373-MG (human glioblastoma) cells using anti- [Catalog # NB600-1384].](http://images.novusbio.com/fullsize/LC3B-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB600-1384-img0030.jpg)
![Analysis of U87MG glioma xenografts using anti- [Catalog # NB600-1384]. Image from verified customer review.](http://images.novusbio.com/fullsize/LC3B-Antibody---BSA-Free-Immunohistochemistry-Paraffin-NB600-1384-img0023.jpg)
![Immunocytochemistry/ Immunofluorescence: LC3B Antibody - BSA Free [NB600-1384] - Assesment of functional basal autophagy in vitro(A) Immunoblotting of LC3B & p62 upon pharmacological autophagy inhibition. A dose-dependent increase of LC3B & p62 was observed with increasing concentrations of chloroquine. (B) Immunofluorescence of LC3B & p62 upon pharmacological autophagy inhibition. I. In CC cell lines HT-29 & II. LoVo a dose-dependent increase of LC3B & p62 was observed with increasing concentrations of chloroquine. (C) Electron microscopy of CC cell lines pharmacological autophagy inhibition. I-III. In CC cell line HT-29 a dose-dependent increase of cytoplasmic vesicles was observed with increasing concentrations of CQ. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28903368), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-310202415384116.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - Phosphorylation of AKT & mTOR decreases after treatment with gemcitabine (GCB)A LM7, CCH-OS-D, & K7M3 osteosarcoma cells were treated with 1μM GCB & cell lysates were analyzed by immunoblotting with specific antibodies for AKT, mTOR, p-AKT, & p-mTOR. beta -actin was used as a loading control. Densitometry was performed using ImageJ. B. & C. Following treatment with GCB, lysates were analyzed using the Human Phospho Kinase Antibody Array. The phosphorylation levels of AKT, mTOR, PRAS40, p70S6K, JNK, AMPK, & ERK were evaluated. Densitometry was performed using Image J. Values were graphed as relative fold change. Means ± standard deviation of three independent experiments are shown. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.20308), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-310202415304227.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - Autophagy decreases during striatal development. (A) Representative Western blot images for LC3B, p62, DARPP32, & actin. Quantification of (B) LC3B-ii relative to actin, (C) LC3B-ii relative to LC3B-i, (D) p62 relative to actin normalized to P120 values. Data analyzed with one-way ANOVA; (B) Age: F(4,21) = 6.526, p = 0.0014; (C) Age: F(4,22) = 3.797, p = 0.0171; (D) Age: F(4,15) = 3.762, p = 0.0260. *p 0.01); (b) FTC-133/TPC-1 cells transfected with HMGB1 shRNA & control shRNA were starved by HBSS for 3 h & then treated with rapamycin (1 μM) for 12 h. Flow cytometry was performed for measuring the ROS level by a DCFH-DA probe in indicated cells. Rap, rapamycin. (n = 3, *P 0.01); (c) FTC-133/TPC-1 cells were transfected with HMGB1 shRNA & control shRNA & then starved by HBSS for 3 h. ATP levels were detected by ATP Assay Kit (n = 3, *P > 0.01); (d) FTC-133/TPC-1 cells were pretreated with NAC (2 mM) & then starved by HBSS for 3 h. LC3-I/II, NIS, p-AMPK, AMPK, p-mTOR, mTOR, p-p70S6K & p70S6K levels were assayed by Western blot; (e) FTC-133/TPC-1 cells transfected with HMGB1 shRNA & control shRNA were starved by HBSS for 3 h & then treated with rapamycin (1 μM) for 12 h. LC3-I/II, NIS, p-mTOR & mTOR levels were assayed by Western blot. Rap, rapamycin Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31331356), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-31020241617143.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - Serum starvation induces autophagy & apoptosis in endothelial cells.A Evaluation by Hoechst 33342 & propidium iodide (HO/PI) staining of apoptosis & necrosis in HUVECs exposed to normal medium (N) or serum-starved (SS) for 4 h. P values obtained by unpaired t test. n = 10 for each condition. Scale bar = 25 μm. B Quantification of caspase-3 activity in HUVECs exposed to N or SS HUVECs for 1, 2, 3, & 4 h. P values obtained by one-way ANOVA. n = 4 for each condition. C Immunoblot & densitometric analysis of PARP, LC3, & SQSTM1/p62 in HUVECs exposed to N or SS for 1, 2, or 4 h. beta -actin (ACTB) was used as a loading control. P values obtained by unpaired t test (*P 0.01, **P > 0.01); (d) Dynamic uptaking: FTC-133/TPC-1 cells were transfected with HMGB1 shRNA & control shRNA & starved by HBSS for 3 h. Indicated cells were cultured with 175 KBq 131I for 5, l0, 20, 30, 60, 90 & 120 min. The uptake of 131I in indicated cells was detected by a gamma counter; (e) Radionuclide uptaking: FTC-133/TPC-1 cells were transfected with HMGB1 shRNA & control shRNA in the presence or absence of 3-MA (10 mM) treatment for 1 h & then starved by HBSS for 3 h. After 1-h incubating with 131I, the uptake of 131I in indicated cells was detected by a gamma counter (n = 3, *P 0.01); (f) FTC-133/TPC-1 cells transfected with HMGB1 shRNA & control shRNA were starved by HBSS for 3 h & then treated with rapamycin (1 μM) for 12 h. After 1-h incubating with 131I, the uptake of 131I in indicated cells was detected by a gamma counter. Rap, rapamycin. (n = 3, *P 0.01) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31331356), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-310202416161815.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - ROS was sufficient for inducing HMGB1 translocation & enhancing autophagy (a) FTC-133/TPC-1 cells were pretreated with the antioxidant (NAC, 2 mM) for 1 h & then starved by HBSS for 3 h. ROS production was assessed by measuring the fluorescent intensity of DCF on a fluorescent plate reader. Incremental production of ROS was expressed as a percentage of control (n = 3, *P 0.01); (b) FTC-133/TPC-1 cells transfected with HMGB1 shRNA & control shRNA were starved by HBSS for 3 h & then treated with rapamycin (1 μM) for 12 h. Flow cytometry was performed for measuring the ROS level by a DCFH-DA probe in indicated cells. Rap, rapamycin. (n = 3, *P 0.01); (c) FTC-133/TPC-1 cells were transfected with HMGB1 shRNA & control shRNA & then starved by HBSS for 3 h. ATP levels were detected by ATP Assay Kit (n = 3, *P > 0.01); (d) FTC-133/TPC-1 cells were pretreated with NAC (2 mM) & then starved by HBSS for 3 h. LC3-I/II, NIS, p-AMPK, AMPK, p-mTOR, mTOR, p-p70S6K & p70S6K levels were assayed by Western blot; (e) FTC-133/TPC-1 cells transfected with HMGB1 shRNA & control shRNA were starved by HBSS for 3 h & then treated with rapamycin (1 μM) for 12 h. LC3-I/II, NIS, p-mTOR & mTOR levels were assayed by Western blot. Rap, rapamycin Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31331356), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-310202416182641.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - Fucoxanthin activated autophagy after TBI.(A) Representative images of immunofluorescence for LC3 surrounding the injured cortex. LC3 punctate dots were observed in the cytoplasm by immunofluorescent staining of LC3 (red). Neuron cells & nuclei are labeled with NeuN (green) & DAPI (blue), respectively. Magnification: 40 x. Scale bar: 50 mm. (B) Mice brain tissues were collected 1 day after TBI in different groups, & the expression of LC3, Beclin-1 & p62 was measured by western blot. Fucoxanthin treatment significantly increased the level of LC3-II & Beclin-1 while decreasing the level of p62 after TBI. (C) 3-MA (400 nM) was injected i.c.v. 30 min before TBI. Mice were then subjected to TBI & treatment of fucoxanthin 30 min after TBI. Pretreatment with 3-MA significantly attenuated fucoxanthin-induced activation of autophagy & suppression of apoptosis & oxidative stress in the ipsilateral cortex. Data are presented as mean ± SEM, n = 6 per group; **p 0.01, **P > 0.01); (d) Dynamic uptaking: FTC-133/TPC-1 cells were transfected with HMGB1 shRNA & control shRNA & starved by HBSS for 3 h. Indicated cells were cultured with 175 KBq 131I for 5, l0, 20, 30, 60, 90 & 120 min. The uptake of 131I in indicated cells was detected by a gamma counter; (e) Radionuclide uptaking: FTC-133/TPC-1 cells were transfected with HMGB1 shRNA & control shRNA in the presence or absence of 3-MA (10 mM) treatment for 1 h & then starved by HBSS for 3 h. After 1-h incubating with 131I, the uptake of 131I in indicated cells was detected by a gamma counter (n = 3, *P 0.01); (f) FTC-133/TPC-1 cells transfected with HMGB1 shRNA & control shRNA were starved by HBSS for 3 h & then treated with rapamycin (1 μM) for 12 h. After 1-h incubating with 131I, the uptake of 131I in indicated cells was detected by a gamma counter. Rap, rapamycin. (n = 3, *P 0.01) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31331356), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-31020241616376.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - Metformin treatment increases cisplatin effects; (A) MDA-MB-231 & Ca Ski cells were either left untreated or treated with metformin or cisplatin alone or metformin in combination with cisplatin for 15 days. At the end of the treatment, cells were processed to obtain whole cell lysates. MAP1LC3B, pPRKAA2Thr172, PRKAA2 & CASP3 (cleaved) expression was determined by Western blot. ACTB was used as loading control. Densitometric analysis of the gels was performed as described under Materials & Methods; (B) MDA-MB-231 & Ca Ski cells were either left untreated or treated with metformin or cisplatin alone or metformin in combination with cisplatin for 15 days. Ammonia level in the culture medium was measured as indicated in the Material & Methods section. # Significantly different from treatment with metformin alone. All experiments in this figure were repeated three times. * Significantly different from control untreated cells. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30646605), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-31020241618938.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - Autophagy & the proteasome regulate CagA stability. (A) Wild-type (WT) & autophagy-deficient (Atg5−/−) MEFs were infected with a CagA+ vacA− isogenic mutant strain (MOI 100) for 8 hours using a gentamycin protection assay. The autophagy marker LC3-II was used to confirm that Atg5−/− MEFs are autophagy-deficient. CagA protein levels were measured by Western blotting using beta -actin as loading control. Graph shows fold change of CagA normalized to beta -actin relative to WT MEFs (mean + SEM; n = 4). (B) AGS cells were infected with a CagA+ vacA− isogenic mutant strain (MOI 50) for 19 hours using a gentamycin protection assay. MG132 (5 μM) was added during the 14-hour low-dose gentamycin incubation. DMSO was used as a vehicle control. CagA protein levels were measured by Western blotting using beta -actin as loading control. Graph shows fold change of CagA normalized to beta -actin relative to vehicle control (mean + SEM; n = 6). (C) AGS cells were infected with a CagA+ vacA− isogenic mutant strain (MOI 50) for 24 hours using a gentamycin protection assay. Lactacystin (10 μM) was added during the 19-hour low-dose gentamycin incubation. Water was used as a vehicle control. CagA protein levels were measured by Western blotting using beta -actin as loading control. Graph shows fold change of CagA normalized to beta -actin relative to vehicle control (mean + SEM; n = 5). Relevant gel bands were cropped from the original blots. Dotted line indicates slicing of two regions together from the same blot. Statistical analysis was performed using Student’s t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30631092), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-310202416173533.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - Vps34 activity is required for maintaining LC3B-ii levels at P10 & mTOR inhibition increases p-Beclin-1 & LC3B-ii levels at P28. (A) Representative Western blot images for actin, DARPP32 & LC3B-i & -ii in striatal slices obtained from P10 or P28 mice, treated with SAR405 (1 μM) or vehicle (Veh; DMSO, 0.1%). (B,C) Quantification of LC3B-ii relative to actin, normalized to vehicle condition at each age. (B) P10: unpaired, two-tailed t-test, t11 = 2.985, p = 0.0124; P28: unpaired, two-tailed t-test, t24 = 1.807, p = 0.0922. P10: Veh: n = 6 slices, SAR405 n = 7 slices from 3 to 4 mice/age. (C) P28: Veh: n = 9 slices, Baf n = 7 slices from 3 to 4 mice/age. *p 0.05 versus untreated group). C. Morphological features of NB4 cells that were treated with ATRA (1 μM) or HMGB1 (1 μg/ml) was determined by Wright-Giemsa staining & visualized by light microscopy (100X magnification). D. Differentiation of NB4 cells treated with ATRA (1 μM) or HMGB1 (10 μg/ml) for 6-48 h was examined by NBT reduction & surface CD11b expression in comparison to the control (DMSO) (n=3, *P<0.05 versus ATRA group). E. Expression of PML-RAR alpha , P62 & LC3-I/II in NB4 cells treated with ATRA (1 μM) or HMGB1 (10 μg/ml) for 48 h was assayed by western blotting & co-immunoprecipitation in comparison to control (DMSO). Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.15432), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-310202416171499.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - Zearalenone (ZEN) induced endoplasmic reticulum (ER) stress & autophagy in HepG2 cells. mRNA level & protein expression were determined by quantitative real-time polymerase chain reaction (qRT-PCR) & Western blot analysis, respectively. (A) The protein expression level of GRP78 was measured in cells treated with ZEN for 1 h. (B) The phosphorylation of eIF2 alpha was evaluated in cells treated with ZEN for 2 h. (C) CHOP mRNA levels, (D) Beclin1 mRNA levels, & (E) LC3-II mRNA levels were determined in cells treated with ZEN for 4 h. (F) The protein expression level of LC3-II/LC3-I was examined in cells treated with ZEN for 24 h. Data represent mean ± SEM of three independent experiments. * indicates significant difference vs. the control (** p < 0.01, & *** p < 0.001). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31861425), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-310202416154612.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - ATRA induces autophagy in SKBR3 cells. (a) SKBR3 & MDA-MB-453 breast cancer cells were treated either with 0.1 or 1 μM ATRA for 2 & 4 days, respectively. beta -Catenin & LC3B levels were measured by western blotting. GAPDH was used as a loading control. (b) LC3B-II quantification from at least three independent experiments. LC3B-II expression was normalized to GAPDH & to vehicle-treated SKBR3 cells. (c) beta -Catenin staining of SKBR3 & MDA-MB453 cells. Cells were control or ATRA (1 μM) treated for 2 days. beta -Catenin FITC (fluorescein isothiocyanate) & nuclear DAPI (4',6-diamidino-2-phenylindole) staining as analyzed by confocal microscopy are shown. (d) Quantification of endogenous LC3B puncta. LC3B in SKBR3 & MDA-MB453 cells treated with 1 μM ATRA for 2 days. (e) LC3B-II western blotting & quantification of the autophagic activation upon treatment with 1 μM ATRA for 2 days in the presence or absence of BafA for 2 h at 200 nM. LC3B-II levels were normalized to GAPDH & to vehicle-treated SKBR3 cells. Standard deviations for five independent experiments are shown. (f) Long-lived protein degradation assay of SKBR3 & MDA-MB453 cells treated as in (e). Radioactivity was determined by liquid scintillation counting of at least three independent experiments. Absolute proteolysis is shown. (g) Long-lived protein degradation assay of SKBR3 treated as in (e) & including treatment with the macroautophagy-specific inhibitor 3-MA (10 mM). Analysis as in (f). Mann–Whitney U-test: *P<0.05, **P<0.01, ***P<0.001 & ****P<0.0001 Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/cddis2015236), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-31020241616052.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - CA1 Tg mice undergo mitochondrial stress. a WB analysis of extracts from 6-mo Wt & Tg mice CA1 (Wt, n = 6; Tg, n = 7), using antibodies against SIRT3, SOD2 & acetylated SOD2. b WB analysis of extracts from 12-mo Wt & Tg mice hippocampi (Wt, n = 5; Tg, n = 5). Data are presented as mean ± SEM (**P < 0.01; ***P < 0.001). WB analysis of extracts from 6-mo Wt & Tg mice CA1 (Wt, n = 6; Tg, n = 5) (c), & from 12-mo Wt & Tg mice hippocampi (Wt, n = 5; Tg, n = 5) (d) for PINK1 & LC-3. Data are presented as mean ± SEM, *P < 0.05. WB analysis of extracts from 6-mo WT & Tg mice CA1 (WT, n = 5; Tg, n = 6) (e), & from 12-mo WT & Tg mice hippocampi (WT, n = 5; Tg, n = 5) (f) for TFAM. Data are presented as mean ± SEM (*P < 0.05), **P < 0.01). Actin was used as loading control Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32131898), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-31020241616181.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - ATRA induces autophagy in SKBR3 cells. (a) SKBR3 & MDA-MB-453 breast cancer cells were treated either with 0.1 or 1 μM ATRA for 2 & 4 days, respectively. beta -Catenin & LC3B levels were measured by western blotting. GAPDH was used as a loading control. (b) LC3B-II quantification from at least three independent experiments. LC3B-II expression was normalized to GAPDH & to vehicle-treated SKBR3 cells. (c) beta -Catenin staining of SKBR3 & MDA-MB453 cells. Cells were control or ATRA (1 μM) treated for 2 days. beta -Catenin FITC (fluorescein isothiocyanate) & nuclear DAPI (4',6-diamidino-2-phenylindole) staining as analyzed by confocal microscopy are shown. (d) Quantification of endogenous LC3B puncta. LC3B in SKBR3 & MDA-MB453 cells treated with 1 μM ATRA for 2 days. (e) LC3B-II western blotting & quantification of the autophagic activation upon treatment with 1 μM ATRA for 2 days in the presence or absence of BafA for 2 h at 200 nM. LC3B-II levels were normalized to GAPDH & to vehicle-treated SKBR3 cells. Standard deviations for five independent experiments are shown. (f) Long-lived protein degradation assay of SKBR3 & MDA-MB453 cells treated as in (e). Radioactivity was determined by liquid scintillation counting of at least three independent experiments. Absolute proteolysis is shown. (g) Long-lived protein degradation assay of SKBR3 treated as in (e) & including treatment with the macroautophagy-specific inhibitor 3-MA (10 mM). Analysis as in (f). Mann–Whitney U-test: *P<0.05, **P<0.01, ***P<0.001 & ****P<0.0001 Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/cddis2015236), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-310202416182623.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - Bmi‐1 deficiency aggravates cardiac hypertrophy & decreases autophagic flux. (A) Representative micrographs of paraffin‐embedded heart ventricular wall sections of 6‐week‐old Bmi‐1–/– mice & WT mice stained for haematoxylin‐eosin (H&E), wheat germ agglutinin (WGA) & Masson's trichrome (Masson) staining. (B) Heart weight relative to body weight (HW/BW) & heart weight relative to tibia length (HW/TL). (C) The wall thickness of interventricular septum. (D) Myocyte cross‐sectional area from Bmi‐1–/– mice relative to WT mice. (E) Collagenous fibre area from Bmi‐1–/– mice relative to WT mice was counted with anterior wall staining for Masson. (F) Anp, Bnp, beta ‐MHC, c‐TnI & GATA4 mRNA levels in hearts by real‐time RT‐PCR, calculated as ratio to beta ‐actin mRNA & expressed relative to WT. (G) Western blots of cardiac tissue extracts & mouse embryonic cardiomyocytes (MECs) showing ANP, BNP, GATA4, LC3B & p16; beta ‐actin was the loading control. (H) Protein levels relative to beta ‐actin were assessed by densitometric analysis. (I) Representative micrographs of paraffin‐embedded heart sections immunohistochemical staining for ANP, BNP & GATA4. (J) The percentage of cells positive for ANP, BNP, GATA4 or positive area relative to total cells or area. (K) Representative micrographs of fluorescence with autophagy lentivirus transfection, with DAPI for nuclei. (L) Percentage of positive GFP dots or mRFP dots relative to total cells. (M) The number of autophagosomes & autolysosomes per cell. Six mice per group were used for experiments. Cell experiments were performed with three biological repetitions per group. Values are mean ± SEM from six determinations per group, *p < .05, **p < .01, ***p < .001 compared with WT group, unpaired Student's t‐test Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35390228), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-31020241618262.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - 8-Cl-Ado-induces autophagy. Immunoblot analysis of (A) phospho-ULK (Ser555) levels & (B) LC3B-I lipidation to form LC3B-II in MCF-7 & BT-474 cells treated with 10 μM of 8-Cl-Ado for the indicated times. (C) Fluorescent microscopy of MCF-7 & BT-474 cells transiently transfected with GFP-LC3B & treated with 10 μM of 8-Cl-Ado for 12-hours to assess aggregation of LC3B. (D) Immunoblot analysis of p62 levels in MCF-7 & BT-474 cells treated with 10 μM of 8-Cl-Ado for the indicated times. The normalized ratio of p62 to GAPDH relative to the untreated control is indicated beneath each lane. (E) Fluorescent microscopic imaging of autolysosomes. MCF-7 cells were untreated or treated for 2-days with 8-Cl-Ado or rapamycin. Cells were stained with MDC, blue, to visualize AVO & Syto 61 (DNA), red, for nuclei counterstaining. (F) Representative flow cytometery histograms of AVO stained with acridine orange in MCF-7 cells untreated or treated for 3 days with 50 nM rapamycin or 10 μM 8-Cl-Ado. Baf was added before 30 min prior to staining to neutralize AVO staining. (G) Quantification triplicate experiments of MCF-7 & BT-474 cells treated & analyzed as in E. Image collected & cropped by CiteAb from the following publication (//jhoonline.biomedcentral.com/articles/10.1186/1756-8722-7-23), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-31020241617525.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - PB induces autophagy but blocks autophagosome trafficking & autophagosome-lysosome fusion in Hep3B cells.(A) Hep3B cells, HepG2 cells, & primary mouse hepatocytes treated w/ increasing concentrations of PB (6–2000 μg/mL) for 24 h; viable cells quantified using the MTT assay. Data are presented as mean ± SD from at least 3 independent experiments. Bars = SD. *P < 0.05, **P < 0.01, ***P < 0.001, control versus PB-treated cells. (B) Hep3B cells treated for 6, 24 & 48 h w/ indicated concentrations of PB. Levels of protein expression analysed by WB using antibodies against LC3B, p62/SQSTM1, ATG12, BECN1 & Actin. Images cropped from different blots run under the same experimental conditions. The original blots attached as Supplementary Figure 3A. (C) Hep3B cells transfected w/ GFP-LC3B treated w/ 240 μg/mL PB for 24 h & then observed under a confocal microscope. (D) Hep3B cells treated for 24 h w/ indicated concentrations of PB. Levels of protein expression analysed by WB using antibodies against phosphorylated & total mTOR, 4EBP1, & p70S6K1 as well as actin. Images cropped from different blots run under the same experimental conditions. The original blots attached as Supplementary Figure 3B. (E) Hep3B cells serum-starved overnight, & incubated w/ or w/out PB (240 μg/mL) for 6 h before stimulating w/ 20 ng/mL EGF for 20 min. EGFR protein levels analysed by confocal microscope. (F) Hep3B cells treated PB for 12, 24 or 48 h w/ indicated concentrations. Levels of protein expression analysed by WB using antibodies against EGFR & Actin. Images cropped from different blots run under the same experimental conditions in each panel. The original blots attached as Supplementary Figure 3C. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/srep41437), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-31020241618948.jpg)
![Dual RNAscope ISH-IHC: Survivin Antibody [NB500-201] - Formalin-fixed paraffin-embedded tissue sections of human esophagus squamous cell carcinoma were probed for Survivin mRNA (ACD RNAScope Probe, [465361]; Fast Red chromogen, ACD [322360]). Adjacent tissue section was processed for immunohistochemistry using rabbit polyclonal [NB500-201] at 1.5ug/mL with overnight incubation at 4 degrees Celsius followed by incubation with anti-rabbit IgG VisUCyte HRP Polymer Antibody [VC003] and DAB chromogen (yellow-brown). Tissue was counterstained with hematoxylin (blue). Specific staining was localized to tumor cells.](http://images.novusbio.com/fullsize/Survivin-Antibody-Dual-RNAscope-ISH-IHC-NB500-201-img0026.jpg "<b>Orthogonal Strategies Validation. </b>Dual RNAscope ISH-IHC: Survivin Antibody [NB500-201] - Formalin-fixed paraffin-embedded tissue sections of human esophagus squamous cell carcinoma were probed for Survivin mRNA (ACD RNAScope Probe, [465361]; Fast Red chromogen, ACD [322360]). Adjacent tissue section was processed for immunohistochemistry using rabbit polyclonal [NB500-201] at 1.5ug/mL with overnight incubation at 4 degrees Celsius followed by incubation with anti-rabbit IgG VisUCyte HRP Polymer Antibody [VC003] and DAB chromogen (yellow-brown). Tissue was counterstained with hematoxylin (blue). Specific staining was localized to tumor cells.")
![<b>Biological Strategies Validation, Genetic Strategies Validation and Orthogonal Strategies Validation.</b>Western Blot: Survivin Antibody [NB500-201] - Western blot analysis using Survivin and flotillin antibodies was performed on lysates of DMSO- and PTX-treated MDAMB231 cells ectopically expressing either control siRNA or Survivin siRNA (panels labeled WCL), as well as on the exosomes these cells generated (panels labeled Exos). Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/2072-6694/8/12/111) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Survivin-Antibody-Knockdown-Validated-NB500-201-img0037.jpg)
![Immunohistochemistry: Survivin Antibody [NB500-201] - Protein expression pattern of Survivin in HCC tissues and non-neoplastic liver parenchyma. IAP members immunoreactivity was estimated by tissue microarray in a subset of HCC patients (n = 40). A-D, Representative Survivin cytoplasmatic immunostaining in a tumor core (A), in a tumor proximal to cirrhosis (C, N: cirrhosis, K: HCC), and in adjacent and long-distance non-neoplastic parenchyma (B and D, respectively). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/19397802) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Survivin-Antibody-Immunohistochemistry-NB500-201-img0038.jpg)
![<b>Genetic Strategies Validation. </b>Knockdown Validated: Survivin Antibody [NB500-201] - Anti-tumor effects and functional evidence of sCA-survivin-siRNA in HCT116 and HT29 solid tumor models. Immunostaining of survivin in the tumor tissues on day 19 using [NB500-201]. Scale bar, 50 um. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0116022) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Survivin-Antibody-Knockdown-Validated-NB500-201-img0033.jpg)
![Immunocytochemistry/Immunofluorescence: Survivin Antibody [NB500-201] - Analysis using the HRP conjugate of [NB500-201]. Staining of Telophase with accumulation of survivin in the midbodies of two daughter cells. Survivin detection using [NB500-201].](http://images.novusbio.com/fullsize/Survivin-Antibody-Immunocytochemistry-Immunofluorescence-NB500-201-img0018.jpg)
![Western Blot: Survivin Antibody [NB500-201] - Analysis of 30ug of HeLa whole cell lysate [NB800-PC1] using rabbit polyclonal [NB500-201] at 1ug/ml. Detection was performed using ECL method with 1 minute exposure. Band detected at higher molecular weight than the predicted MW (16 kDa).](http://images.novusbio.com/fullsize/Survivin-Antibody-Western-Blot-NB500-201-img0017.jpg)
![Immunohistochemistry-Paraffin: Survivin Antibody [NB500-201] - Immunohistochemical staining of Survivin in human rectal cancer using [NB500-201] and DAB with hematoxylin counterstain.](http://images.novusbio.com/fullsize/Survivin-Antibody-Immunohistochemistry-Paraffin-NB500-201-img0008.jpg)
![Flow Cytometry: Survivin Antibody [NB500-201] - An intracellular stain was performed on HeLa cells with [NB500-201] and a matched isotype control. Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550.](http://images.novusbio.com/fullsize/Survivin-Antibody-Flow-Cytometry-NB500-201-img0025.jpg)
![Western Blot: Survivin Antibody [NB500-201] - Western blot analysis using Survivin Antibody [NB500-201]. Effects of siRNA transfection on the expression of Bcl-xL and survivin. Bcl-xL and survivin protein content detected by Western Blotting 48 h after transfection. Bcl-xL and survivin levels are shown normalized to the reference protein beta-actin and relative to the ns-si control. Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/1422-0067/14/6/12297) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Survivin-Antibody-Western-Blot-NB500-201-img0032.jpg)
![Western Blot: Survivin Antibody [NB500-201] - Analysis of Survivin in human hepatocytes from cancer patient (left) and HeLa cell lysate (right) using [NB500-201]. Image from verified customer review. Note: bands detected at higher molecular weight than predicted (16 kDa)](http://images.novusbio.com/fullsize/Survivin-Antibody-Western-Blot-NB500-201-img0013.jpg)
![Western Blot: Survivin Antibody [NB500-201] - Western blot analysis using [NB500-201]. Survivin protein is degraded by ubiquitin proteasome in serum-free and serum-containing media. Western blots and protein quantitation graphs showing that addition of MG-132 proteasome inhibitor (10 uM) extended survivin protein half-life in serum-free and serum-containing media. One representative western blot out of triplicate experiments was shown for each treatment and condition. *Indicates the time at which survivin protein is half of the amount at 0 hours (half-life), P 100. ** p-value 100. ** p-value < .01 using student t-test. H. PFGE analysis of EBV episomes & linears at 7 days post-transduction with lentivirus shRNA for shControl or shSurvivin in MUTU I or RAJI cell lines. Human alpha satellite DNA is used for DNA loading control Western blot of Survivin & Actin are shown below for each cell at 7 days post-transduction. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28077791), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb500-201_rabbit-polyclonal-survivin-antibody-310202416171444.jpg)
![Western Blot: Survivin Antibody - BSA Free [NB500-201] - The p53-p21 axis facilitates downregulation of survivin via cell cycle(A) HCT116 wild typeand p21-deficient (p21-/-) cells were treated with 5 μM L-OHP for 24 hours. Whole cell lysates were analyzed with antibodies against p53, p21, & survivin; vinculin serves as loading control. (B) Cell cycle distribution was analyzed after 24 hours treatment by flow cytometry analysis (n = 3). (C) To induce p21, RKO p21ind cells were treated with 3 nM Muristerone A for 24 hours & tested for the levels of p21 & survivin; vinculin, loading control. (D)BIRC5 mRNA levels were analyzed by quantitative real-time PCR after 24 hours treatment with MurA in RKO p21ind cells (n = 3). (E) Cell cycle distribution was measured by flow cytometry analyses of cellular DNA content (n = 3). (F) Scheme summarizing the supposed mechanisms of survivin regulation after L-OHP & CPT-11 treatment. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29963241), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb500-201_rabbit-polyclonal-survivin-antibody-310202416182643.jpg)
![Western Blot: Survivin Antibody - BSA Free [NB500-201] - Apoptosis & survival signaling after L-OHP & CPT-11(A) Western blot analysis using antibodies against p53 & pro-apoptotic BAX & PIG-3 after treatment with 5 μM L-OHP or 10 μM CPT-11. (B) Immunodetection of NF-kappa B p65, RELB & anti-apoptotic survivin, XIAP, BCL-XL & MCL1; vinculin serves as loading control. (C) Effects of increasing doses L-OHP & CPT-11 on caspase-3 & PARP1 cleavage after 24 hours treatment; alpha -tubulin serves as loading control. (D) Cells were treated with a combination of L-OHP & the caspase-inhibitor Z-VAD-FMK (50 μM). Immunodetection of survivin, p53 & full-length caspase-3 was conducted. Detection of apoptosis was determined by cleavage products of caspase-3 & PARP1; beta -actin serves as loading control. Please note: Figure 4A & 4B, as well as Supplementary Figure 2A show signals acquired by different detection methods, but originate from the same Western blots. This is due to a switch in the immunoblot chemiluminescence detection system from X-ray films (darker background) to a CCD camera system (Fusion Solo S, Vilber Lourmat; lighter background). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29963241), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb500-201_rabbit-polyclonal-survivin-antibody-310202416175291.jpg)
![Western Blot: Survivin Antibody - BSA Free [NB500-201] - Anti-tumor effects & functional evidence of sCA-survivin-siRNA in HCT116 & HT29 solid tumor models.(A) For western blot analysis, HCT116 cells were seeded into 6-well plates & transfected with 100 pmol/well of either control or survivin siRNA by Lp (Lipofectamine 2000) or sCA. Actin blots served as loading controls. (B) For proliferation assays, cells were uniformly seeded into 96-well plates (1 × 104 cells/well), & 5 pmol/well siRNA was used. Cell viability was examined at 48 & 72 h by WST-8 assay. Data represent mean ± SEM. *P = 0.0294, **P = 0.0304 (n = 4, Wilcoxon rank test). (C) In vivo tumor growth. Each vehicle, carrying 15 μg of control siRNA or survivin siRNA, was administered by intravenous injection to mice with HCT116 tumors. Data represent the mean ± SEM (n = 10 tumors, Wilcoxon rank test). (D) Immunostaining of survivin in the tumor tissues on day 19. Scale bar, 50 μm. (E) In vivo live imaging of sCA-siRNA (6-FAM labeled) in HT29 tumor by multiphoton microscopy at 90 min. (F) Fluorescent detection of naked-siRNA (6-FAM labeled) or sCA-siRNA (6-FAM labeled) in the HT29 tumor at 4 h. Green: 6-FAM labeled siRNA; Red: microvasculature; Blue: DAPI stained nuclei. Scale bar, 50 μm. (G) Mice were administered with 40 μg of naked-survivin-siRNA or sCA-survivin-siRNA on days 0, 1, & 2. Tumors were removed on day 3, & western blot analysis for survivin was performed. (H) Many tumor cells treated with sCA-survivin-siRNA (6-FAM labeled) had condensed nuclei & were positive for TUNEL assay. Scale bar, 50 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25738937), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb500-201_rabbit-polyclonal-survivin-antibody-310202416175225.jpg)
![Western Blot: Survivin Antibody - BSA Free [NB500-201] - Survivin is essential for the salinomycin-induced apoptosis in UM cells. a UM cells were treated with salinomycin for 24 h & the protein levels of apoptosis-related proteins were detected by Western blot. b & c UM cells were transduced with lentiviral pTSB-Survivin cDNA (b), Survivin-shRNA constructs (c), or their corresponding empty vectors, & then incubated in the presence of puromycin (1 μg/mL) for 5 days to reach stable clones. Such survivin-manipulated cells were then exposed to salinomycin for 24 h, & subjected to trypan blue exclusion assay (left) & Western blot assay (right). Data represent mean ± SD. ns, not significant; *, P < 0.05; **, P < 0.01; ***, P < 0.001, Student’s t test. d qRT-PCR analysis of BIRC5 mRNA level was done in the 92.1 & Mel270 cells treated with salinomycin for 24 h. **, P < 0.01; ***, P < 0.001, one-way ANOVA, post hoc comparisons, Tukey’s test Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31718679), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb500-201_rabbit-polyclonal-survivin-antibody-310202416161820.jpg)
![Immunocytochemistry/ Immunofluorescence: Survivin Antibody - BSA Free [NB500-201] - Anti-tumor effects & functional evidence of sCA-survivin-siRNA in HCT116 & HT29 solid tumor models.(A) For western blot analysis, HCT116 cells were seeded into 6-well plates & transfected with 100 pmol/well of either control or survivin siRNA by Lp (Lipofectamine 2000) or sCA. Actin blots served as loading controls. (B) For proliferation assays, cells were uniformly seeded into 96-well plates (1 × 104 cells/well), & 5 pmol/well siRNA was used. Cell viability was examined at 48 & 72 h by WST-8 assay. Data represent mean ± SEM. *P = 0.0294, **P = 0.0304 (n = 4, Wilcoxon rank test). (C) In vivo tumor growth. Each vehicle, carrying 15 μg of control siRNA or survivin siRNA, was administered by intravenous injection to mice with HCT116 tumors. Data represent the mean ± SEM (n = 10 tumors, Wilcoxon rank test). (D) Immunostaining of survivin in the tumor tissues on day 19. Scale bar, 50 μm. (E) In vivo live imaging of sCA-siRNA (6-FAM labeled) in HT29 tumor by multiphoton microscopy at 90 min. (F) Fluorescent detection of naked-siRNA (6-FAM labeled) or sCA-siRNA (6-FAM labeled) in the HT29 tumor at 4 h. Green: 6-FAM labeled siRNA; Red: microvasculature; Blue: DAPI stained nuclei. Scale bar, 50 μm. (G) Mice were administered with 40 μg of naked-survivin-siRNA or sCA-survivin-siRNA on days 0, 1, & 2. Tumors were removed on day 3, & western blot analysis for survivin was performed. (H) Many tumor cells treated with sCA-survivin-siRNA (6-FAM labeled) had condensed nuclei & were positive for TUNEL assay. Scale bar, 50 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25738937), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb500-201_rabbit-polyclonal-survivin-antibody-310202416182634.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - Morphological alterations induced by DMOG are HIF-1alpha dependent. glEND.2 cells were stably transfected with shGFP, shHIF-1alpha or shHIF-2alpha. The clones were cultured under normoxic (N) or hypoxic (H, 1% O2) conditions, or treated with DMOG for 6 h. 30 ug protein of cellular protein were loaded for the detection of HIF-1alpha, and nuclear extracts (20 ug protein) were used for the detection of HIF-2alpha. Image collected and cropped by CiteAb from the following publication (//biosignaling.biomedcentral.com/articles/10.1186/1478-811X-11-80) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Knockdown-Validated-NB100-449-img0050.jpg "<b>Genetic Strategies Validation. </b>Western Blot: HIF-1 alpha Antibody [NB100-449] - Morphological alterations induced by DMOG are HIF-1alpha dependent. glEND.2 cells were stably transfected with shGFP, shHIF-1alpha or shHIF-2alpha. The clones were cultured under normoxic (N) or hypoxic (H, 1% O2) conditions, or treated with DMOG for 6 h. 30 ug protein of cellular protein were loaded for the detection of HIF-1alpha, and nuclear extracts (20 ug protein) were used for the detection of HIF-2alpha. Image collected and cropped by CiteAb from the following publication (//biosignaling.biomedcentral.com/articles/10.1186/1478-811X-11-80) licensed under a CC-BY license.")
![<b>Biological Strategies Validation and Genetic Strategies Validation.</b>Western Blot: HIF-1 alpha Antibody [NB100-449] - HIF-1 alpha induction on Caki-1 cell lysate using CoCl2. Image from verified customer review.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Western-Blot-NB100-449-img0015.jpg)
![Simple Western: HIF-1 alpha Antibody [NB100-449] - Simple Western lane view shows a specific band for HIF-1 alpha in 0.5 mg/ml of hypoxic HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Simple-Western-NB100-449-img0032.jpg)
![Immunohistochemistry: HIF-1 alpha Antibody [NB100-449] - Mouse Brain, Neurons 40X](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Immunohistochemistry-NB100-449-img0034.jpg)
![Immunohistochemistry: HIF-1 alpha Antibody [NB100-449] - Detection of human HIF1-alpha by immunohistochemistry. Sample: FFPE section of renal cell carcinoma. Antibody: Affinity purified rabbit anti-HIF1-alpha antibody (NB110-58773). Detection: DAB](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Immunohistochemistry-NB100-449-img0047.jpg)
![<b>Biological Strategies Validation. </b>Western Blot: HIF-1 alpha Antibody [NB100-449] - Detection of Human HIF-1 alpha by Western Blot and Immunoprecipitation. Samples: Whole cell lysate (5, 15 and 50 ug for WB; 1 mg for IP, 20% of IP loaded) from HeLa cells that were either treated with cobalt chloride (+; 200 uM) or mock treated (-). Antibodies: Affinity purified rabbit anti-HIF1 alpha antibody used for WB at 0.1 ug/mL(A) and 1 ug/mL (B) and used for IP at 3 ug/mg lysate. HIF-1 alpha was also immunoprecipitated by a previous lot of this antibody. Detection: Chemiluminescence with exposure times of 30 seconds (A) and 10 seconds (B).](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Western-Blot-NB100-449-img0038.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - Blot showing the effect of hypoxia on the protein expression levels of the purine biosynthetic enzymes. HIF-1 alpha is stabilized in hypoxia as expected, and no significant increase in the purine enzymes was detected between normoxic (21% oxygen) and hypoxic (1% oxygen) growth conditions. The positions of molecular markers surrounding each band of interest are shown for each blot. ADSL (NBP2-03107), ATIC (NBP2-01941), FGAMS (NBP1-84691), GART (H00002618-M01), HIF-1a (NB100-449), PAICS (NBP2-02817), PPAT (NBP2-02056). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32439803/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Western-Blot-NB100-449-img0053.jpg)
![Immunocytochemistry/Immunofluorescence: HIF-1 alpha Antibody [NB100-449] - Murine primary bone marrow derived macrophages stained with HIF1-alpha antibody (red). Nuclei were counterstained with DAPI (blue). Image from verified customer review.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Immunocytochemistry-Immunofluorescence-NB100-449-img0039.jpg)
![Immunohistochemistry-Paraffin: HIF-1 alpha Antibody [NB100-449] - Analysis of microvascular density and HIF-1alpha activity. Low, homogenous expression of HIF-1alpha was detected in the tumors of NNK treated mice (40X, scale bar = 25 um). Image collected and cropped by CiteAb from the following publication (//molecular-cancer.biomedcentral.com/articles/10.1186/1476-4598-11-4), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Immunohistochemistry-Paraffin-NB100-449-img0052.jpg)
![Flow Cytometry: HIF-1 alpha Antibody [NB100-449] - HeLa cells were treated for 15 hrs with 200 uM CoCl2, fixed in PFA, and permeabilized in 90% MeOH. 1 X 10^6 cells were stained with 0.125 ug anti-HIF-1 alpha and secondary FITC-conjugated goat anti-rabbit (in a 150 uL reaction). Black: treated, anti-KLH control IgG; Red: untreated, anti-HIF-1 alpha; Blue: treated, anti-HIF-1 alpha.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Flow-Cytometry-NB100-449-img0035.jpg)
![<b>Biological Strategies Validation. </b>Western Blot: HIF-1 alpha Antibody [NB100-449] - Analysis of HIF-1 alpha in human myeloma cell lysate using anti-HIF-1 alpha. Cells were untreated or treated with IGF-1, IL-6 or CoCl2. Image from verified customer review.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Western-Blot-NB100-449-img0033.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - Detection of HIF-1 alpha in a hypoxic sample. Lane 1: CoCl2 treated Cos-7 nuclear extract (hypoxic). Lane 2: Untreated Cos-7 nuclear extract (normoxic).](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Western-Blot-NB100-449-img0036.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - Detection of mouse HIF-1 alpha on hypoxia treated MEFs](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Western-Blot-NB100-449-img0037.jpg)
![<b>Biological Strategies Validation. </b>Western Blot: HIF-1 alpha Antibody [NB100-449] - Samples: Whole cell lysate (5, 15 and 50 ug) from HeLa cells that were treated with cobalt chloride (+; 200 uM) or mock treated (-). Antibodies: Affinity purified rabbit anti-HIF1 alpha antibody NB100-449 used for WB at 0.1 ug/ml. Detection: Chemiluminescence with exposure times of 30 seconds.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Western-Blot-NB100-449-img0042.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - BMDM were seeded at 0.5x10^6 overnight. Cells were treated with 10 ng/ml LPS for 24 hrs. Image from verified customer review.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Western-Blot-NB100-449-img0043.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - Analysis of total protein using anti-HIF-1 alpha, -CAIX, -ISCU antibodies and VDACs antibody (PMID: 29596470).](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Western-Blot-NB100-449-img0044.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - Analysis of total protein using anti-HIF-1 alpha, -ISCU, -FXN antibodies. CoCl2 was used to treat or not HeLa cells for 2 days (PMID: 29596470).](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Western-Blot-NB100-449-img0045.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - Detection of human HIF1 alpha by western blot. Samples: Whole cell lysate (15 and 50 ug) from HEK293T cells that were either treated with 200 uM cobalt chloride (+) or mock treated (-). Antibodies: Affinity purified rabbit anti-HIF1 alpha antibody NB100-449 used for WB at 0.1 ug/ml. Detection: Chemiluminescence with exposure times of 3 minutes.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Western-Blot-NB100-449-img0046.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - 3T3-L1 mouse embryonic fibroblast adipose-like cell line. Antibody at 1:2000. WB image submitted by a verified customer review.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Western-Blot-NB100-449-img0051.jpg)
![<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: HIF-1 alpha Antibody [NB100-449] - Formaldehyde-fixed asynchronous HeLa cells.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Immunocytochemistry-Immunofluorescence-NB100-449-img0006.jpg)
![Immunoprecipitation: HIF-1 alpha Antibody [NB100-449] - HIF-1 alpha analysis in HEK293 cells. Image from verified customer review.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Immunoprecipitation-NB100-449-img0005.jpg)
![Immunoprecipitation: HIF-1 alpha Antibody [NB100-449] - Detection of human HIF1 alpha by western blot of immunoprecipitates. Samples: Whole cell lysate (1 mg for IP, 20% of IP loaded) from HEK293T cells that were treated with 200 uM cobalt chloride. Antibodies: Affinity purified rabbit anti-HIF1 alpha antibody NB100-449 used for WB at 1 ug/ml and for IP at 6 ug/mg lysate. Detection: Chemiluminescence with exposure times of 3 minutes.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Immunoprecipitation-NB100-449-img0048.jpg)
![Immunohistochemistry: HIF-1 alpha Antibody [NB100-449] - Analysis of microvascular density & HIF-1 alpha activity. Microvascular density of pulmonary tumors was significantly higher in hyperplastic (B) & tumoral lesions (D) of NNK/NTHi treated mice compared to the NNK treated mice (A, & C) detected by CD105 immunostaining (10X, scale bar = 100 μm). HIF-1 alpha immunostaining after NNK/NTHi combined treatment showed hot-spots of high stromal expression in tumors (F), & high expression in perivascular-peribronchiolar lymphocytes (H). In contrast, low, homogenous expression of HIF-1 alpha was detected in the tumors (E) & perivascular-peribronchiolar lymphocytes (G) of NNK treated mice (40X, scale bar = 25 μm). Image collected & cropped by CiteAb from the following publication (//molecular-cancer.biomedcentral.com/articles/10.1186/1476-4598-11-4), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-310202415284545.jpg)
![Immunocytochemistry/ Immunofluorescence: HIF-1 alpha Antibody [NB100-449] - Chronic ethanol feeding enhances tumorigenesis markers during AOM/DSS-induced tumorigenesis. AOM/DSS-induced colonic tumorigenesis was induced with (EF) or without (PF) 4 % ethanol feeding as described in Methods section. Cryosections of distal colon were stained for VEGF (a) pSmad (b), or HIF1 alpha (c), & co-stained for F-actin & nucleus. Images presented are representative of n of 5 for each group Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26951793), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-310202415304212.jpg)
![Immunohistochemistry-Paraffin: HIF-1 alpha Antibody [NB100-449] - Treatment with HBOT or PFD decreased HIF-1 alpha expression in the AD lesions.IHC for HIF-1 alpha (A). Scale bar is 100 µm. HIF-1 alpha + area was measured in five fields chosen at random by using image analysis software (B). RT-PCR for HIF-1 alpha (C). NT, not treated. Data are expressed as the mean ± SD (n = 12). *P<0.05, compared with the control group; ¶P<0.05, compared with the AD-NT group; §, P<0.05, compared with the AD-Steroid group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25275529), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-310202415363719.jpg)
![Immunohistochemistry-Paraffin: HIF-1 alpha Antibody [NB100-449] - Elevated PIK3/AKT/HIF-1 alpha pathways in KL SqCC tumours.(a,b) Analysis of TCGA gene expression (normalized TPM) & PIK3CA (a) & PTEN (b) genomic copy number alteration profiles. Each dot represents one SqCC patient (n=501). Boxes represent the interquartile range & whiskers are drawn to the minimum & maximum. Kruskal–Wallis non-parametric ANOVA, ****P<0.0001, ***P<0.001, **P<0.01. (c) IHC analysis (top) & quantification (bottom) of p63, p-AKT, p-S6, p-4EBP1, HIF-1 alpha & GLUT1 in KL tumours (n=6 each group). Two-tailed t-test, ****P<0.0001, ***P<0.001, **P<0.01. Scale bar, 50 μm. (d) Immunoblot analysis of HIF-1 alpha & GLUT1 in control shGFP & shHIF-1 alpha knockdown SqCC cell lines, HCC95 & HCC1588. All error bars represent the mean±s.e.m. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28548087), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-31020241534344.jpg)
![Immunohistochemistry: HIF-1 alpha Antibody [NB100-449] - Analysis of microvascular density & HIF-1 alpha activity. Microvascular density of pulmonary tumors was significantly higher in hyperplastic (B) & tumoral lesions (D) of NNK/NTHi treated mice compared to the NNK treated mice (A, & C) detected by CD105 immunostaining (10X, scale bar = 100 μm). HIF-1 alpha immunostaining after NNK/NTHi combined treatment showed hot-spots of high stromal expression in tumors (F), & high expression in perivascular-peribronchiolar lymphocytes (H). In contrast, low, homogenous expression of HIF-1 alpha was detected in the tumors (E) & perivascular-peribronchiolar lymphocytes (G) of NNK treated mice (40X, scale bar = 25 μm). Image collected & cropped by CiteAb from the following publication (//molecular-cancer.biomedcentral.com/articles/10.1186/1476-4598-11-4), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-310202415384135.jpg)
![Immunohistochemistry: HIF-1 alpha Antibody [NB100-449] - Immunolocalization of HIF1A in limbs.Immunoreactivity was detected in control limbs in the apical ectodermal ridge & interdigital regions (I.R.). The mesenchymal condensations/developing cartilaginous anlagen (Digits) were not immunoreactive. 4-OOHCPA treatment resulted in a concentration- & time-dependent increase in HIF1A immunoreactivity in this area in the 3 & 6 h exposure groups; staining was diminished by 24 h. Four separate replicates were done. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0051937), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-310202415293325.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - Effects of cell stress on VEGF-A & HIF1 alpha expression in Müller cells & Y79 photoreceptors. (A) VEGF-A was measured by ELISA using conditioned media collected from MIO-M1 & Y79 cells, n = 4–5/group in Müller cells & n = 8/group in Y79 photoreceptors, ** p < 0.01; (B) Western blots for HIF1 alpha using cellular proteins, n = 4/group, ** p < 0.01. For MIO-M1 Müller cells: Grey bars: 5 mM glucose. Black bars: 25 mM glucose. For Y79 photoreceptors: Grey bars: 11 mM glucose. Black bars: 25 mM glucose. NS, not significant; LG, low glucose; HG, high glucose. Image collected & cropped by CiteAb from the following publication (//www.mdpi.com/1422-0067/18/3/533), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-310202415394514.jpg)
![Immunohistochemistry: HIF-1 alpha Antibody [NB100-449] - Analysis of microvascular density & HIF-1 alpha activity. Microvascular density of pulmonary tumors was significantly higher in hyperplastic (B) & tumoral lesions (D) of NNK/NTHi treated mice compared to the NNK treated mice (A, & C) detected by CD105 immunostaining (10X, scale bar = 100 μm). HIF-1 alpha immunostaining after NNK/NTHi combined treatment showed hot-spots of high stromal expression in tumors (F), & high expression in perivascular-peribronchiolar lymphocytes (H). In contrast, low, homogenous expression of HIF-1 alpha was detected in the tumors (E) & perivascular-peribronchiolar lymphocytes (G) of NNK treated mice (40X, scale bar = 25 μm). Image collected & cropped by CiteAb from the following publication (//molecular-cancer.biomedcentral.com/articles/10.1186/1476-4598-11-4), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-310202415291950.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - Phenylhydrazine administration results in hypoxia in retinal vessels & in HIF-1 alpha & HIF-2 alpha stabilization in peripheral blood leukocytes.(A) 3-dimensional reconstructed imaging of the superficial vascular plexus of flat mounted retinae of mice (steady state, treated with PHZ & treated with PHZ & peak EIU induction) stained with DAPI, hypoxyprobe & Isolectin B4. (B) Representative analysis of HIFs by western blot: 50ug of protein from total cell lysate of blood leukocytes isolated from mice treated with PHZ compared to untreated; (C) relative densitometry quantification of HIF western blots from PBMC showing mean, n = 3, error bar showing SD, unpaired t test, ***P < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28112274), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-310202415304256.jpg)
![Immunohistochemistry-Frozen: HIF-1 alpha Antibody [NB100-449] - Ethanol elevates tumorigenic markers & nuclear localization of HIF1 alpha in colonic crypts during AOM/DSS-induced tumorigenesis: AOM/DSS-induced colonic tumorigenesis was induced with or without 4 % ethanol feeding as described in Methods section. a & b Colonic mucosal extracts were immunoblotted for pSmad & VEGF (a), & the band density evaluated using Image J software (b). Values are mean ± SE (n = 3). Asterisks indicate the values that are significantly different (p < 0.05) from corresponding values for AOM/DSS group. c Cryosections of colon were stained for HIF1 alpha (red) & nucleus (blue). Sections of the images from Fig. 2c are enlarged to show the detailed localization of HIF1 alpha in the nucleus. While arrows indicate nuclear co-localization of HIF1 alpha Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26951793), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-31020241553383.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - Dectin-1-induced NADPH oxidase-derived ROS is required for augmented IL-1 beta during TSLPR inhibition. (A) Human mDC derived from healthy donors (HD) or CGD patients were stimulated with SC glucan for 8 h (n = 2 representative donors presented, three separate experiments performed). Pro-IL-1 beta , IL-1 beta , HIF-1 alpha , phospho-AMPK, AMPK & beta -actin were measured by immunoblot. (B–E) Densitometry of cumulative data was performed using Image Studio Lite software with pro-IL-1 beta , IL-1 beta & HIF-1 alpha normalized to beta -actin & phospho-AMPK normalized to total AMPK. Data is reported as percentage of maximal signal observed within each donor (n = 3 independent donors, presented as pooled data). (F–H) Human mDC derived from HD or CGD patients were stimulated with SC glucan, CA glucan or heat killed C. albicans hyphae with anti-TSLPR or IgG isotype control antibodies for 24 h (n = 3 independent donors, presented as pooled data). IL-1 beta was measured in 24-h cell culture supernatants by ELISA. Cumulative data displayed as mean +SEM. Statistical analysis calculated using one-way ANOVA with Bonferroni post-tests (***p = 0.001,*p = 0.05). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31139177), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-310202415532021.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - Reactive oxygen species production & expression of stabilized HIF1 alpha & AMPK subunit alpha 2 & in H1299 & H1299r cells(A) H1299, H1299r, P31 & P31r cell were seeded at a density of 250,000 cells/well & left for 24 h. The cells were then stained with 10 μmol/L dichloro-dihydro-fluorescein diacetate (DCFH-DA). Fluorescence was analysed for 10,000 events. Whole cell lysates were prepared from confluent cultures of H1299, H1299r cells. Proteins (90 μg) were resolved in 10% SDS-PAGE gels & transferred to a PVDF membrane. (B) Representative blot of HIF1 alpha protein expression. (C) Representative blot of AMPK subunit alpha 2 protein expression from four independent experiments. (D) Bar chart of AMPK subunit alpha 2 mean for four separate measurements. Statistical analyses was carried out using the student t-test. ** = p<0.01, * = p<0.05. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.21885), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-310202415525284.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - Pyruvate kinase isoform M2 (PKM2) & hypoxia-inducible factor 1 alpha (Hif-1 alpha ) bind directly to the promoter region of PDL1 in primary murine BMDM cells. BMDM cells were treated with TEPP-46 at 50 µM for 1 h prior to stimulation with LPS (100 ng/ml, 24 h) (A). Binding of PKM2 (left) or Hif-1 alpha (right) to HRE1 or HRE4 of the PD-L1 promoter was detected by incubating cell lysates with biotinylated oligonucleotides spanning the relevant HRE promoter region. Protein–oligonucleotide complexes were isolated using streptavidin agarose beads, & proteins were detected by western blotting. Representative of n = 3. Chromatin immunoprecipitation (ChIP)-PCR (B) using PKM2 & HIF-1 alpha antibodies & primers specific for three promoter regions of PD-L1 (HRE1, 2–3, & 4) & a known Hif-1 alpha binding region of vascular endothelial growth factor as a positive control showing binding of Hif-1 alpha (left) & PKM2 (right) to the PD-L1 promoter in LPS-treated BMDMs (100 ng/ml, 24 h). (C) Sequential ChIP assays measuring simultaneous endogenous binding of PKM2 & Hif-1 alpha to chromatin in response to LPS (100 ng/ml, 24 h) ±TEPP-46 (pretreatment using 50 µM, 60 min). ChIP data are calculated as percent of input, error bar represents mean ± SEM, & statistics are performed as two-tailed unpaired t-test *P < 0.05, **P < 0.01, & ***P < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29081778), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-31020241612685.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - Changes in Hepatic Oxygen Saturation & Hypoxia-related Protein Expression. (A) In the representative case, the hepatic oxygen saturation in the experimental group was lower than that in the control group at four, six, & eight weeks (51.6 vs. 54.5%, 48.4 vs. 53.9%, 32.3 vs. 43.2%, & 31.2 vs. 42.9%). (B) There was significant decrease of oxygen saturation of liver parenchyma in the experimental group compared to those of control group (45.2 vs. 51.9%, 43.0 vs. 49.0%, & 31.3 vs. 49.7%) at the four, six, & eight weeks, respectively (P < 0.001). (C) In the Western blot analysis, the experimental group was relatively higher expression of hypoxia-inducible factor-1 alpha (HIF-1 alpha ) & vascular endothelial growth factor (VEGF) protein than the control group at eight weeks. The full-length blots with these antibodies were presented in supplementary Figure S1. (D,E) The experimental group showed significantly higher expression of HIF-1 alpha & VEGF protein than the control group at eight-week (1.47 ± 0.48 vs. 0.19 ± 0.08 & 0.96 ± 0.23 vs. 0.33 ± 0.06, P = 0.019 & P < 0.018). *P < 0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29079853), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-31020241552391.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - BCAT1 expression & inhibition in human macrophages.(a) RNA-sequencing in human monocyte-derived macrophages (hMDMs) shows mRNA copies of BCAT enzymes in normalized counts. n=14 healthy donor hMDMs were used for RNA-seq. (b) Chemical structure of ERG240 & leucine. (c) Enzymatic activity of recombinant human BCAT1 & BCAT2 in presence of ERG240. (d) Relative expression of IRG1, HIF1A & IL1B measured by qRT-PCR in control, ERG240-treated (20 mM, 3 h), LPS treated (100 ng ml−1, 3 h), & LPS+ERG240 treated (LPS, 100 ng ml−1; ERG240, 20 mM for 3 h) hMDMs. ns, non-significant. All expression values are normalized to those obtained for HPRT gene expression. n=3 healthy donor hMDMs were used in each group. (e) Western blot analysis of IRG1, IL-1 beta , HIF-1 alpha & beta-actin (ACTB) in control (untreated), ERG240-treated (20 mM, 3 h), LPS treated (100 ng ml−1, 3 h) & LPS+ERG240 treated (LPS, 100 ng ml−1; ERG240, 20 mM for 3 h) hMDMs. The experiment is representative of three independent experiments using n=3 healthy donor hMDMs each. (f) GC/MS results showing itaconic acid production in hMDMs in presence or absence of ERG240 (20 mM). LPS treatment was for 8 h (100 ng ml−1). GC/MS plot for each donor is shown separately where itaconate abundance denotes arbitrary units. Error bars are s.e.m. Significance was tested using two-tailed Student’s t-test or one-way ANOVA. * P<10−3 following two-way ANOVA. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/ncomms16040), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-31020241554543.jpg)
![Immunocytochemistry/ Immunofluorescence: HIF-1 alpha Antibody [NB100-449] - HIF-1 alpha /2 alpha expression in myeloid-specific KO mice targeting the HIF pathway. (A) Images of the colon of wild-type (WT), myeloid-specific Hif-1a KO (hMRP8 Hif-1a KO) or von Hippel Lindau (Vhl) KO (hMRP8 Vhl KO) mice, immunostained for MRP8 (green) & the DNA-binding regions of Hif-1a mRNA (red). Mice were fed with 5% DSS for 4 days prior to immunostaining analyses. Note that there were no MRP8-positive cells that were positive for Hif-1a mRNA in hMRP8 Hif-1a KO (middle column) mice, but we observed many cells that were double positive for MRP8 & Hif-1a mRNA in hMRP8 Vhl KO mice (right column). (B) Images of the colon of hMRP8 Vhl KO mice fed with 5% DSS as in A, immunostained for MRP8 (green) & HIF-1 alpha (red, upper row) or HIF-2 alpha (red, bottom row). DAPI-stained nuclei are shown in blue. White boxes in A & B indicate the regions magnified in the lower or right images, respectively. Yellow arrowheads in A & B indicate cells positive for both markers. Scale bars: 100 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29967068), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-31020241554544.jpg)
![Immunocytochemistry/ Immunofluorescence: HIF-1 alpha Antibody [NB100-449] - Increased infiltration of myeloid cells expressing HIF-1 alpha in DSS-induced colitis. (A) Western blot analysis of MRP8, F4/80 or actin using the whole colon tissue lysate from mice fed with water or 5% DSS for 4 days. (B) Images of the colon of mice fed with water or 5% DSS, immunostained for myeloid cells using anti-MRP8 (green) or anti-HIF-1 alpha (red) antibodies. Nuclei were counterstained with DAPI. White rectangles indicate the areas magnified in the images shown below. Yellow arrowheads indicate cells with colocalization of MRP8 & HIF-1 alpha . Quantification of MRP8-positive cells & percentage of those expressing HIF-1 alpha are shown as bar graphs on the right-hand side. Data are mean±s.e.m. for at least three independent fields examined per mouse (n≥3 per group). **P<0.01 & ***P<0.001, assessed by Student's t-test. HPF, high-powered field. (C) Images of the colon of mice fed with 5% DSS, immunostained for MRP8 (red) & CD11b (green). DAPI-stained nuclei are shown in blue & a merged image is also shown. Scale bars: 100 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29967068), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-31020241612613.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - Increased HIF-1 alpha expression is regulated by TSLPR inhibition & not IL-1 beta secretion (A) Human mDC were stimulated with SC glucan with either anti-TSLPR or IgG isotype control antibodies for 8 h in the presence or absence of IL-1 beta neutralization antibodies (n = 1 representative donor presented, three separate experiments performed). Pro-IL-1 beta , IL-1 beta , HIF-1 alpha , phospho-p38 MAPK, p38 MAPK, phospho-AMPK, AMPK & beta -actin were measured by immunoblot. (B,C) Densitometry of cumulative data was performed using Image Studio Lite software with HIF-1 alpha normalized to beta -actin & phospho-AMPK normalized to AMPK. Data is reported as percentage of maximal signal observed within each donor (n = 3 independent donors, presented as pooled data). Cumulative data displayed as mean +SEM. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31139177), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-31020241612635.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - miR-18b (miR-18b-5p) regulates Hif1 alpha & reduces apoptosis in mtNSC-34 cells. a Overexpressed miR-18b (miR-18b-5p) decreased Hif1 alpha & Mef2c proteins. Both Mctp1 & Rarb expression were increased by miR-18b (miR-18b-5p). Downregulated Bax & upregulated Bcl2 by miR-18b (miR-18b-5p) diminished apoptosis in mtNSC-34 cells. b RT-qPCR analysis showed low expression of Hif1 alpha & Mef2c mRNAs. c Mctp1 & Rarb transcripts were highly expressed by miR-18b (miR-18b-5p). d Bax mRNAs were decreased & Bcl2 mRNAs were increased by overexpressed miR-18b. e miR-18b (miR-18b-5p) was overexpressed in mtNSC-34 cells. f miR-206 was reduced by miR-18b (miR-18b-5p). g LDH release analysis explained that transfected miR-18b (miR-18b-5p) restores apoptosis. h Luciferases assay with 3′ UTR of Hif1 alpha showed that Hif1 alpha is target of miR-18b in contNSC-34 cells. i & j Overexpression of miR-18b (miR-18b-5p) enhanced neuronal differentiation (MAP2) & attenuated intracellular Ca2+ levels (Cont (0.098) versus miR-18b (miR-18b-5p) (0.051) in fluorescence intensities from baseline 490/525 ratio) in mtNSC-34 cells. Empty vector served as a negative control (Cont). Arrow represents SOD1 aggregation (green). Scale bar, 40 μm. Significantly different at *, p < 0.05; **, p < 0.005. The experiments were replicated 5 times Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32605607), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-3102024155453.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - Hypoxic conditions upregulate CNN3 in BeWo cells.BeWo cells were cultured either under normoxic or under hypoxic conditions for 24(A) Total protein lysates were examined with the Western Blot technique to detect CNN3 protein levels. For normalization, HPRT was stained on the same membrane. As hypoxia marker, HIF-1 alpha was detected as well. (B) Protein bands of CNN3 & HPRT were densitometrically measured on the Western Blot membrane & CNN3/HPRT levels are plotted in the graph (white column: normoxia; black column: hypoxia). n = 3. (C) BeWo cells were serum starved for 16 h & then treated with either PBS as control or 200 µM CoCl2 for 6 h in serum free medium. Then total protein was isolated & a Western Blot was performed. The HIF-1 alpha, CNN3 & HPRT protein was detected on the membrane with specific antibodies. (D) A densitometric analysis was performed to determine CNN3/HPRT levels (white column: normoxia; black column: hypoxia). n = 3. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25050546), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-31020241554521.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - Dynamics of the hypoxia-triggered decrease in MET phosphorylation & its reversal upon reoxygenation(A) MCF10A cells were incubated under normoxia or hypoxia for 1 h. They were then treated, under the same oxygen pressure, with 10 ng/mL HGF/SF for 5, 10, 20, 30, 60, 90 & 120 minutes. A control (Ctrl) without any HGF/SF stimulation was also performed. The same amount of protein was analyzed by western blotting with antibodies directed against: phosphorylated residues in the MET kinase domain, the MET kinase domain, the hypoxia marker HIF1a, phosphorylated Akt, Akt, Erk2, phosphorylated Erk, & actine. The positions of prestained molecular weight markers are indicated. Arrows indicate the positions of precursor & mature full-length MET. (B) MCF10A cells were incubated under hypoxia for 5, 10, 15 or 30 minutes. Another set of cells were incubated under hypoxia for 1 h & then returned to normoxia for 5, 10, 15 or 30 min (re-oxygenation). A control under normoxic (N) conditions was also included. The same amount of protein was analyzed by western blotting as previously described with the addition of GAB1 & its phosphorylated form. (C) MCF10A cells were placed under normoxic or hypoxic conditions for 1 h or hypoxia for 1 h & then normoxia for 10 minutes (reoxygenation). Cells were then treated at the indicated time with 10 ng/mL of HGF/SF. Cell lysates were incubated for AlphaScreen specific phospho-Erk & phospho-Akt quantitation. Error bars represent standard deviations (n = 3; ± SD). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29930749), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-31020241552522.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - The role of HIF-1 in purinosome formation.a, quantifying the number of purinosome-containing cells in normoxia or hypoxia (24 h) in purine-rich medium & normoxia in purine-depleted medium (purine -ve), cells in hypoxia transfected with siRNA to HIF-1 alpha (+ siRNA), & cells in purine-rich medium supplemented with DFX. Data shown are n = 3, mean ± S.E., total number of cells counted are shown in parentheses. b, time course of purinosome formation in hypoxia shows the number of purinosome-containing cells steadily increases after 3 h in hypoxia. Re-oxygenation of the samples after hypoxic incubation for 10 h reverts the number purinosome-containing cells back to normoxic levels. Data shown is n = 3, mean ± S.E., total number of cells counted are shown in parentheses. c, time course of HIF-1 alpha stabilization in hypoxia shows maximum HIF-1 alpha protein expression levels at 3 h in hypoxia, after which the HIF-1 alpha expression decreases. The positions of molecular markers are shown for each blot; uncropped blots with overlaid markers are deposited in the raw data files. d, the effect of hypoxia on the transcription of purine biosynthesis enzymes measured by qPCR. Vascular endothelial growth factor (VEGF) & HIF-1 alpha are controls. Data shown are n = 5, mean ± S.E. e, the effect of hypoxia on the protein expression levels of the purine biosynthetic enzymes. HIF-1 alpha is stabilized in hypoxia as expected, & no significant increase in the purine enzymes was detected between normoxic (21% oxygen) & hypoxic (1% oxygen) growth conditions. The positions of molecular markers surrounding each band of interest are shown for each blot; uncropped blots with overlaid markers are deposited in the raw data files. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32439803), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-31020241682187.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - C/EBPδ promotes HIF-1 alpha expression in macrophages through inhibition of FBXW7 alpha a) RT-PCR analysis of FBXW7 isoform expression from different sources as follows. 1, primary peritoneal macrophages (PPMs); 2, RAW 264.7 cells; 3, MMTV-Neu mammary tumour tissue; 4, primary mouse embryo fibroblasts. Numbers indicate the position of size markers in base pairs. (b) RT-qPCR analysis of Fbxw7 transcript levels in PPMs from WT & Cebpd−/− KO mice, cultured +/− LPS (100 ng/ml, 24 h), compared to WT untreated (n=4, *P<0.05; **P<0.001). (c) Western analysis of nuclear extract (NE) from primary human monocytes nucleofected with siRNA oligos (C, control; D, CEBPD; F, FBXW7) & treated with LPS (100 ng/ml) & 1%O2 (16 h) as indicated. SE, short exposure; LE, long exposure. (d) RT-qPCR analysis of FBXW7 & CEBPD transcripts in primary human monocytes as in panel (c) (n=3, *P<0.05; **P<0.001). (e) Western analysis of NE from PPMs nucelofected with siRNA oligos & treated with LPS (100 ng/ml) & 1%O2 for 16 h as indicated. SE, short exposure; LE, long exposure.Where applicable, data are mean±S.E.M., evaluated by two-tailed unequal variance t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23575666), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-31020241683944.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - Hypoxia downregulates CFTR expression. (a) Phase-contrast photographs of MDCK cells treated with normoxia & hypoxia conditions; (b) Western blot showing downregulation of CFTR in the MDCK cells by hypoxia (Full-length blot is shown in Supplementary Figure S7b.); (c) Real time-PCR assay showing decreased mRNA expression of CFTR induced by hypoxia in HK-2 cells,*p < 0.05; (d) Western blot showing decreased expression of CFTR induced by hypoxia in HK-2 cells (Full-length blot is shown in Supplementary Figure S7c.); (e) Western blot showing the expression changes of HIF-1 alpha & EMT markers induced by hypoxia in MDCK cells, quantification analysis is shown in the lower panel, *p < 0.05; (Full-length blot is shown in Supplementary Figure S7d.) (f) Immunofluorescent staining showing dramatically increased HIF-1 alpha & reduced CFTR protein levels in tubular epithelial cells at inner cortices in UUO kidney (arrow). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28701694), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-31020241612654.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - NRP1 & MET on HT1080 cells are accessible for blood-borne rhodocetin-alpha beta (A) expression of NRP1 & MET by HT1080 cells was proven by flow cytometry. Gray, isotype-matched controls. (B) flow cytometry of NRP1-knockout HT1080 cells demonstrating their NRP1-deficiency & unaffected MET expression. (C) treatment with CoCl2, mimicking a hypoxic tumor micro-environment, induced upregulation of HIF-1 alpha . (D) NRP1, as a downstream target of HIF-1 alpha , is upregulated in HT1080 cells but not in NRP1-knockout HT1080 cells. beta -actin immunoblots show even loading. (E) increased HIF-1 alpha (red) levels in hypoxic tumor regions, which also contained partly (arrows) or completely (open arrows) EC-deficient VM vessels. ECs are stained green & nuclei blue. (F) immunostaining of NRP1 (red) & MET (blue) showed that both proteins were present on HT1080 cells & ECs in tumor tissue. Note the continuity between EC-lined vasculature & EC marker-deficient vessels (arrows in F’). F’, F’’, in oblique view, gating of the green CD31 signal also showed an apical absence of NRP1 on ECs in contrast to MET (open arrows). (G) the fluorescence intensity along a traceroute, averaged over a width of 5 pixels, (rectangle in F) through the endothelium revealed that in ECs NRP1, unlike MET, is absent from the apical side & restricted to the basolateral side. In contrast, on ATV/VM-lining cells (F’, arrows) both NRP1 & MET are accessible from the bloodstream (H). Vertical gray lines in G & H indicate the position of the apical cell border. Original magnification was 400× (E) & 630× (F-F’’). Representative images are shown. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.25032), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-310202415533837.jpg)
![Immunohistochemistry: HIF-1 alpha Antibody [NB100-449] - NRP1 & MET on HT1080 cells are accessible for blood-borne rhodocetin-alpha beta (A) expression of NRP1 & MET by HT1080 cells was proven by flow cytometry. Gray, isotype-matched controls. (B) flow cytometry of NRP1-knockout HT1080 cells demonstrating their NRP1-deficiency & unaffected MET expression. (C) treatment with CoCl2, mimicking a hypoxic tumor micro-environment, induced upregulation of HIF-1 alpha . (D) NRP1, as a downstream target of HIF-1 alpha , is upregulated in HT1080 cells but not in NRP1-knockout HT1080 cells. beta -actin immunoblots show even loading. (E) increased HIF-1 alpha (red) levels in hypoxic tumor regions, which also contained partly (arrows) or completely (open arrows) EC-deficient VM vessels. ECs are stained green & nuclei blue. (F) immunostaining of NRP1 (red) & MET (blue) showed that both proteins were present on HT1080 cells & ECs in tumor tissue. Note the continuity between EC-lined vasculature & EC marker-deficient vessels (arrows in F’). F’, F’’, in oblique view, gating of the green CD31 signal also showed an apical absence of NRP1 on ECs in contrast to MET (open arrows). (G) the fluorescence intensity along a traceroute, averaged over a width of 5 pixels, (rectangle in F) through the endothelium revealed that in ECs NRP1, unlike MET, is absent from the apical side & restricted to the basolateral side. In contrast, on ATV/VM-lining cells (F’, arrows) both NRP1 & MET are accessible from the bloodstream (H). Vertical gray lines in G & H indicate the position of the apical cell border. Original magnification was 400× (E) & 630× (F-F’’). Representative images are shown. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.25032), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-31020241612628.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - C/EBPδ promotes HIF-1 alpha expression in macrophages through inhibition of FBXW7 alpha a) RT-PCR analysis of FBXW7 isoform expression from different sources as follows. 1, primary peritoneal macrophages (PPMs); 2, RAW 264.7 cells; 3, MMTV-Neu mammary tumour tissue; 4, primary mouse embryo fibroblasts. Numbers indicate the position of size markers in base pairs. (b) RT-qPCR analysis of Fbxw7 transcript levels in PPMs from WT & Cebpd−/− KO mice, cultured +/− LPS (100 ng/ml, 24 h), compared to WT untreated (n=4, *P<0.05; **P<0.001). (c) Western analysis of nuclear extract (NE) from primary human monocytes nucleofected with siRNA oligos (C, control; D, CEBPD; F, FBXW7) & treated with LPS (100 ng/ml) & 1%O2 (16 h) as indicated. SE, short exposure; LE, long exposure. (d) RT-qPCR analysis of FBXW7 & CEBPD transcripts in primary human monocytes as in panel (c) (n=3, *P<0.05; **P<0.001). (e) Western analysis of NE from PPMs nucelofected with siRNA oligos & treated with LPS (100 ng/ml) & 1%O2 for 16 h as indicated. SE, short exposure; LE, long exposure.Where applicable, data are mean±S.E.M., evaluated by two-tailed unequal variance t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23575666), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-310202415533827.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - Dectin-1-induced TSLP negatively regulates pro-IL-1 beta & HIF-1 alpha . (A) Human mDC were stimulated with SC glucan, CA glucan or heat killed C. albicans hyphae with anti-TSLPR antibodies or IgG isotype control for 24 h (n = 6 independent donors, presented as pooled data). Lactate production was measured in cell-culture supernatants using colourmetric L-lactate detection kit. (B) Human mDC were stimulated SC glucan with either anti-TSLP, anti-TSLPR or IgG isotype control antibodies for 8 h (n = 1 representative donor presented, three separate experiments performed). Pro-IL-1 beta , IL-1 beta , HIF-1 alpha , phospho-p38 MAPK, p38 MAPK, phospho-AMPK, AMPK & beta -actin were measured by immunoblot. (C–G) Densitometry of cumulative data was performed using Image Studio Lite software with pro-IL-1 beta , IL-1 beta & HIF-1 alpha normalized to beta -actin & phospho-p38 MAPK & phospho-AMPK normalized to total p38 MAPK & AMPK respectively. Data is reported as percentage of maximal signal observed within each donor (n = 3 independent donors, presented as pooled data). Cumulative data displayed as mean +SEM. Statistical analysis calculated using one-way ANOVA with Bonferroni post-tests (***p = 0.001). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31139177), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-31020241682146.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - Involvement of MET in Akt & Erk pathway activation under hypoxiaMCF10A cells were transfected with a pool of three MET-targeting siRNAs (20 nM) or a control siRNA (siCtrl). A control without siRNA was also included (Ctrl) (A). MCF10A cells were transfected with two HIF1a-targeting siRNAs (20 nM), independently or together, or a control siRNA (siCtrl) (B). The cells were then placed for 1 h under normoxic or hypoxic conditions & treated or not for 10 min with 10 ng/mL HGF/SF. In each experiment, the same amount of protein was analyzed by western blotting with antibodies directed against: phosphorylated residues in the MET kinase domain, the MET kinase domain, phosphorylated Akt, Akt, phosphorylated Erk, Erk2, phosphorylated GAB1, GAB1, or hypoxia marker HIF1a. The positions of prestained molecular weight markers are indicated. Arrows indicate the positions of precursor & mature full-length MET & Erk1/2 proteins. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29930749), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-31020241682155.jpg)
![Western Blot: HIF-1 alpha Antibody [NB100-449] - beta -Glucan size affects the requirement for reactive oxygen species (ROS) in IL-1 beta induction. (A) Human monocyte-derived dendritic cell (mDC) stimulated with curdlan or glucan-mp for 8 h. ROS were detected by incubating cells with CellRox Green fluorescence dye & analysis by flow cytometry (representative experiment of two) presented, (B) Human mDCs from healthy donors or chronic granulomatous disease (CGD) patients were stimulated with curdlan or glucan-mp for 8 h. HIF-1 alpha & pro-IL-1 beta protein expression measured by immunoblot (n = 2 donors). (C–L) Human mDC from healthy donors or CGD patients were stimulated with curdlan or glucan-mp for 24 h (n = 6 donors). IL-1 beta , IL-6, IL-23, TSLP, & CCL22 secretion were measured by enzyme-linked immunosorbent assay, with cumulative data displayed as mean ± SEM. Image collected & cropped by CiteAb from the following publication (//journal.frontiersin.org/article/10.3389/fimmu.2017.00791/full), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-449_rabbit-polyclonal-hif-1-alpha-antibody-310202415541992.jpg)
![Western Blot: LC3A Antibody - BSA Free [NB100-2331] - LC3A Antibody [NB100-2331] - High autophagosome concentration is consumed during early immortalized human mesenchymal stem cell differentiation. Immortalized human mesenchymal stem cells were differentiated under osteogenic conditions (see Materials and methods) and assayed for changes in LC3I and LC3II during a 72-hour window. Cells were differentiated under standard conditions (top) or with addition of 5 uM rapamycin (middle) or 5 nM bafilomycin (bottom) for the first 3 hours of differentiation to modulate autophagy. Immunoblots were performed for LC3 at the indicated time points to assess autophagosome degradation via relative changes in LC3II (lower band; 17 kDa). Studies were repeated three times with similar trends seen consistently. Image collected and cropped by CiteAb from the following publication (//stemcellres.com/content/5/6/140), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/LC3A-Antibody---BSA-Free-Western-Blot-NB100-2331-img0041.jpg "Western Blot: LC3A Antibody - BSA Free [NB100-2331] - LC3A Antibody [NB100-2331] - High autophagosome concentration is consumed during early immortalized human mesenchymal stem cell differentiation. Immortalized human mesenchymal stem cells were differentiated under osteogenic conditions (see Materials and methods) and assayed for changes in LC3I and LC3II during a 72-hour window. Cells were differentiated under standard conditions (top) or with addition of 5 uM rapamycin (middle) or 5 nM bafilomycin (bottom) for the first 3 hours of differentiation to modulate autophagy. Immunoblots were performed for LC3 at the indicated time points to assess autophagosome degradation via relative changes in LC3II (lower band; 17 kDa). Studies were repeated three times with similar trends seen consistently. Image collected and cropped by CiteAb from the following publication (//stemcellres.com/content/5/6/140), licensed under a CC-BY license.")
![Immunocytochemistry/Immunofluorescence: LC3A Antibody - BSA Free [NB100-2331] - LC3A Antibody [NB100-2331] - Analysis in PFA fixed NIH/3T3 cells using anti-LC3A antibody. Image from verified customer review.](http://images.novusbio.com/fullsize/LC3A-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB100-2331-img0046.jpg)
![Immunohistochemistry: LC3A Antibody - BSA Free [NB100-2331] - LC3A Antibody [NB100-2331] - Staining in mouse meniscus and cartilage. Image from verified customer review.](http://images.novusbio.com/fullsize/LC3A-Antibody---BSA-Free-Immunohistochemistry-NB100-2331-img0045.jpg)
![Western Blot: LC3A Antibody - BSA Free [NB100-2331] - Autophagy mobilized during differentiation of immortalized human mesenchymal stem cells (ihMSCs). Cultured ihMSCs were stimulated to undergo osteogenesis to form osteoblasts for 30 days at 21% and 4% oxygen. LC3I and LC3II levels were assessed via immunoblot every 10 days and normalized to beta-actin to derive average LC3II band densities. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25523618/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/LC3A Antibody - BSA Free-Western Blot-NB100-2331-img0047.jpg)
![Western Blot: LC3A Antibody - BSA Free [NB100-2331] - LC3A Antibody [NB100-2331] - Autophagy mobilized during differentiation of immortalized human mesenchymal stem cells (ihMSCs). Cultured ihMSCs were stimulated to undergo osteogenesis to form osteoblasts for 30 days at 21% and 4% oxygen. LC3I and LC3II levels were assessed via immunoblot every 10 days and normalized to beta-actin to derive average LC3II band densities. Image collected and cropped by CiteAb from the following publication (//stemcellres.com/content/5/6/140), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/LC3A-Antibody---BSA-Free-Western-Blot-NB100-2331-img0036.jpg)
![Western Blot: LC3A Antibody - BSA Free [NB100-2331] - LC3A Antibody [NB100-2331] - This LC3A antibody Image shows Analysis in human cell lysates.](http://images.novusbio.com/fullsize/LC3A-Antibody---BSA-Free-Western-Blot-NB100-2331-img0037.jpg)
![Western Blot: LC3A Antibody - BSA Free [NB100-2331] - LC3A Antibody [NB100-2331] - This LC3A antibody Image shows analysis of heart tissue lysates from mice which were subjected or not to 48 hours of starvation. The signal was developed using ECL method and this LC3 antibody was found to detect both forms of LC3, i.e. LC3A and LC3B. As expected, the levels of LC3B form were higher in the heart tissue lysates from starved mice.](http://images.novusbio.com/fullsize/LC3A-Antibody---BSA-Free-Western-Blot-NB100-2331-img0039.jpg)
![Western Blot: LC3A Antibody - BSA Free [NB100-2331] - LC3A Antibody [NB100-2331] - Detection of HRP conjugated autophagic LC3 in mouse ES cell lysate. The atg5-/- lane (ES cells, cultured to form embryonic bodies, that are deficient in conversion of LC3-1 to LC3-11) demonstrates the specificity of NB 100-2331, as there is no detection of LC3-11. Photo courtesy of Dr. Beth Levine, UT Southwestern Medical Center.](http://images.novusbio.com/fullsize/LC3A-Antibody---BSA-Free-Western-Blot-NB100-2331-img0040.jpg)
![Immunocytochemistry/Immunofluorescence: LC3A Antibody - BSA Free [NB100-2331] - LC3A Antibody [NB100-2331] - This LC3A antibody Image shows an analysis in HeLa cells using anti-LC3 antibody (red). Nuclei were counterstained with DAPI (blue).](http://images.novusbio.com/fullsize/LC3A-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB100-2331-img0038.jpg)
![Immunocytochemistry/Immunofluorescence: LC3A Antibody - BSA Free [NB100-2331] - LC3A Antibody [NB100-2331] - Left panel shows untreated HeLa cells. Right panel shows HeLa cells that were treated with 50 uM CQ overnight. Cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.05% Triton X-100. The cells were incubated with anti-LC3A antibody at 5 ug/mL overnight at 4C and detected with an anti-mouse DyLight 488 (Green) at a 1:500. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/LC3A-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB100-2331-img0042.jpg)
![Immunohistochemistry: LC3A Antibody - BSA Free [NB100-2331] - LC3A Antibody [NB100-2331] - Rapamycin increases autophagy in brains of PDAPP mice. Representative epifluorescent (c200x) image of hippocampal CA1 in control- and rapamycin-fed transgenic PDAPP mice stained with an anti-LC3 antibody. An increase in LC3-immunoreactive puncta was observed in CA1 projections of transgenic PDAPP mice following rapamycin administration. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0009979) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/LC3A-Antibody---BSA-Free-Immunohistochemistry-NB100-2331-img0043.jpg)
![Immunohistochemistry: LC3A Antibody - BSA Free [NB100-2331] - LC3A Antibody [NB100-2331] - Analysis in mouse renal tissue. Image from verifed customer review.](http://images.novusbio.com/fullsize/LC3A-Antibody---BSA-Free-Immunohistochemistry-NB100-2331-img0044.jpg)
![Simple Western: LC3A Antibody - BSA Free [NB100-2331] - LC3A Antibody [NB100-2331] - Image shows a specific band for LC3 in 0.5 mg/mL of Neuro2A lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/LC3A-Antibody---BSA-Free-Simple-Western-NB100-2331-img0025.jpg)
![Western Blot: LC3A Antibody - BSA Free [NB100-2331] - Chronic, third window RIC increases the expression of autophagosome proteins, LC3I/II & Atg5.(A) Western blots for autophagy related signaling proteins. (B) Quantification of the protein fold change in 3W RIC compared to 3W controls. Values are means ± S.E.M. n = 6–8 per group. An (*) denotes a statistically significant difference (P10 larvae/sample). Lc3 c & e, or p62 & Optineurin d protein levels were detected in absence or presence of BafA1, c & d, or in the presence or absence of Mm e. Actin was used as a loading control. Western Blots were repeated three, c & d, or two e times with protein extracts derived from independent experiments. The Lc3II/Actin or p62/Actin & Optineurin/Actin ratio, normalized to the control sample, is indicated below the blots. f–g Representative confocal micrographs & quantification of GFP-Lc3 co-localization with Mm clusters in infected dram1∆19n/∆19n & dram1+/+ larvae. The top images f show the entire region of imaging, while the bottom images f′ & f″ show details of GFP-Lc3 colocalization of Mm clusters in dram1∆19n/∆19n & dram1+/+ larvae. The arrowheads indicate GFP-Lc3-positive Mm clusters. The data is accumulated from two independent experiments (≥15 larvae/group) & represented by scatter & boxplots as detailed in the “Methods” section. Scale bars, 10 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32332700), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2331_rabbit-polyclonal-lc3a-antibody-31020241612632.jpg)
![Western Blot: LC3A Antibody - BSA Free [NB100-2331] - Optn or p62 deficiency affects autophagosome formation.(A) Workflow of the experiments shown in (B-G). Larvae were treated with 100 nM of Baf A1 for 12 h from 3.5 dpf. The GPF-Lc3 negative larvae were selected to assay autophagy activity by Western blot, the GFP-Lc3 positive larvae were collected to monitor autophagic activity using confocal imaging. The red square indicates the region for confocal imaging. (B) Level of basal autophagy in WT & mutant embryos in absence or presence of Baf A1. Protein samples were extracted from 4 dpf WT & mutant larvae (>10 embryos/sample). The blots were probed with antibodies against Lc3 & Actin as a loading control. Western blots were repeated at least three times with independent extracts. (C) Quantification of Lc3-II fold changes in WT & mutant embryos in absence or presence of Baf A1. Western blot band intensities were quantified by Lab Image. Data is combined from three independent experiments. (D) Representative confocal micrographs of GFP-Lc3 puncta present in the tail fin of optn+/+, optn delta 5n/ delta 5n, p62+/+ & p62 delta 37n/ delta 37n at 4 dpf. Scale bars, 10 μm. (E). Quantification of the number of GFP-Lc3 puncta in optn+/+, optn delta 5n/ delta 5n, p62+/+ & p62 delta 37n/ delta 37n larvae with & without Baf A1 treatment. Each larva was imaged at a pre-defined region of the tail fin (as indicated by the red boxed area in Fig3 A) (≥11 larvae/group). Results are accumulated from two independent experiments. ns, non-significant, *p10 larvae/sample). The blots were probed with antibodies against Lc3 & Actin as a loading control & Lc3-II/Lc3-I ratios are indicated below. Western blots were repeated twice with independent extracts. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30818338), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2331_rabbit-polyclonal-lc3a-antibody-310202415541914.jpg)
![Western Blot: LC3A Antibody - BSA Free [NB100-2331] - UBC9 is degraded by autophagy in epithelial cells.(A) Immunolocalization of UBC9 in ultrathin sections of HKs transduced with empty or HPV16 E6/E7 vectors. Original view (left) & higher magnification (right) of boxed regions. Gold particles are selectively enriched in autophagic structures highlighted by arrows. Scale bar = 1 μm. (B) Top: Representative WB of HaCaT cells treated with the indicated autophagic activators (left) & inhibitors (right). Activation of autophagy was monitored by the conversion of LC3 (LC3-I) to the lipidated LC3 (LC3-II) form, a marker of autophagosome production induced by autophagic stimuli [41]. LC3-II accumulation was used to verify autophagic impairment [41]. Bottom: normalized UBC9 expression. Data are expressed as fold over untreated cells. Bars represent means ± SEM of n = 4 different biological replicates. ns: not significant (Kruskal–Wallis one-way ANOVA with Dunn’s post hoc test) compared to vehicle control groups. (C) Representative WB analysis of U-2 OS or MCF7 cells treated with chloroquine. n = 3 different biological replicates. (D) Representative WB analysis of MCF7 cells transduced with scramble or ATG5 shRNA. The observed ATG5 band represents the ATG5-ATG12 conjugated form. LC3-I accumulation is reported to evidence autophagic deficiencies promoted by shATG5. n = 3 replicates of a single transduction. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.ppat.1006262), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2331_rabbit-polyclonal-lc3a-antibody-310202415525247.jpg)
![Western Blot: LC3A Antibody - BSA Free [NB100-2331] - Dram1 is required for GFP-Lc3 targeting to Mm clusters.a, b Representative confocal micrographs & quantification of GFP-Lc3 puncta in dram1∆19n/∆19n & dram1+/+ larvae in an unstimulated situation (basal autophagy, a) & following BafA1 treatment b. Each larva was imaged at a pre-defined region of the tail fin (≥11 larvae/group). Results are accumulated from two independent experiments & represented by scatter & boxplots as detailed in the “Methods” section. ns non-significant, *p 10 larvae/sample). Lc3 c & e, or p62 & Optineurin d protein levels were detected in absence or presence of BafA1, c & d, or in the presence or absence of Mm e. Actin was used as a loading control. Western Blots were repeated three, c & d, or two e times with protein extracts derived from independent experiments. The Lc3II/Actin or p62/Actin & Optineurin/Actin ratio, normalized to the control sample, is indicated below the blots. f–g Representative confocal micrographs & quantification of GFP-Lc3 co-localization with Mm clusters in infected dram1∆19n/∆19n & dram1+/+ larvae. The top images f show the entire region of imaging, while the bottom images f′ & f″ show details of GFP-Lc3 colocalization of Mm clusters in dram1∆19n/∆19n & dram1+/+ larvae. The arrowheads indicate GFP-Lc3-positive Mm clusters. The data is accumulated from two independent experiments (≥15 larvae/group) & represented by scatter & boxplots as detailed in the “Methods” section. Scale bars, 10 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32332700), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2331_rabbit-polyclonal-lc3a-antibody-310202415541920.jpg)
![Western Blot: LC3A Antibody - BSA Free [NB100-2331] - Knockdown of FUT1 is associated with an increase in autophagic flux. (a) Immunoblot analysis of LC3-II & p62 levels in control & FUT1 knockdown cells. Total cell lysates from MCF-7 & T47D cells transfected with control or FUT1 siRNAs were collected at 120 & 96 h post-transfection, respectively. Equal amounts of cell lysates were then loaded in each lane & separated by SDS-PAGE. Immunoblot analysis was performed with LC3 & p62 antibodies. Actin was used as a loading control. The intensity of LC3-II & p62 protein bands on immunoblot were quantified & normalized to actin, & the relative levels of protein expression were expressed as fold change by setting the control group value to 1. Values shown are mean±S.E.M. of three independent experiments (***P100 cells per group (*P<0.05) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27560716), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2331_rabbit-polyclonal-lc3a-antibody-31020241553512.jpg)
![Western Blot: LC3A Antibody - BSA Free [NB100-2331] - Effect of MIR376A overexpression on autophagy.(A) MCF-7 cells were co-transfected with either MIR-CNT (control plasmid) or MIR376A & GFP-LC3 plasmid, & GFP-LC3 dot formation was analyzed. White arrows indicate clusters of the GFP-LC3 dots in cells. (B) Quantification of the experiments in A. MIR376A overexpression, but not MIR-CNT expression, blocked starvation (STV)-induced autophagy (mean ± S.D. of independent experiments, n = 4, ***p<0,01). NON STV, non-starved (C) Overexpression of MIR376A resulted in a decrease in the autophagic activity of MCF-7 cells. Starvation-induced conversion of LC3-I to LC3-II in MCF-7 cells was analyzed. Tests were performed in the presence or absence of E64d (10 µg/ml) & Pepstatin A (10 µg/ml) (E+P). LC3-II/LC3-I densitometric ratios were marked. ACTB was used as a loading control. (D) MIR376A blocked starvation induced SQSTM1 degradation in MCF-7 cells. ACTB was used as a loading control. SQSTM1/ACTIN densitometric ratios were marked. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24358205), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2331_rabbit-polyclonal-lc3a-antibody-310202415535132.jpg)
![Western Blot: LC3A Antibody - BSA Free [NB100-2331] - Tau clearance in vivo & autophagy function. Clearance kinetics of photoconverted Dendra-tau measured in neurons of WT-tau & AT152T-tau fish. Measurement of intensity of red Dendra-tau signal over time reflects the clearance or degradation of tau protein. (C–F) WBs for LC3-II, a well-characterized marker of autophagosome number, demonstrate that there no differences in levels of this protein between WT-tau & A152T-tau fish either at 24 hpf (pre-phenotype; C & D) or 72 hpf (post-phenotype; E & F). (E & F) Measurements of LC3-II levels in presence or absence of ammonium chloride provides a method for measuring autophagic flux. No differences observed between the two transgenic lines at 3 dpf, suggesting that autophagy functions normally in both WT-tau & A152T-tau fish (graph represents mean ± SD of four independent clutches per group for E & F & 3for C & D; two-tailed t-test). Image collected & cropped by CiteAb from the following publication (//academic.oup.com/brain/article/140/4/1128/2980948), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2331_rabbit-polyclonal-lc3a-antibody-31020241682110.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - PPM1H does not dephosphorylate Ser111 of Rab8A or key phosphorylation sites of AMPK & Akt signaling pathways.(A) HEK293 cells were transiently transfected with constructs expressing the indicated components. 24 hr post-transfection, cells were treated ±10 µM CCCP (Carbonyl cyanide m-chlorophenyl hydrazine) for 3 hr to induce activation of the PINK1 kinase & trigger Rab8A phosphorylation at Ser111 (Lai et al., 2015). (B) As in (A) except cells were immunoblotted with the indicated antibodies that recognize key phosphorylation sites of AMPK & Akt signaling pathways. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31663853), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-31020241534312.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - PINK1 & Parkin are phosphorylated after a decrease in delta Ψm in mouse primary neurons. Neurons were infected with lentivirus encoding PINK1-Flag (A), wild-type HA-Parkin (B) or HA-Parkin with either the S65A or S65E mutation (C). Cells were treated with the mitochondrial uncoupler CCCP (30 μm) for 1–3 h & subjected to SDS-PAGE in the absence or presence of 50 μm phos-tag. Note that mobility does not reflect the molecular weight of proteins in phos-tag PAGE (Kinoshita et al. 15), & thus, molecular weight markers are not shown in the bottom gels. The red & black asterisks in (C) indicate phosphorylation of Parkin at Ser65 & an additional minor phosphorylation site, respectively. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23751051), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415384188.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - PINK1 translation is critical for the accumulation of PINK1 upon mitochondrial damage. aPINK1 mRNA levels were not altered by mitochondrial damage. HeLa cells were incubated with 10 μM CCCP or combination of 10 μM oligomycin & 4 μM antimycin for 2 h & then, PINK1 mRNA levels were measured by qRT-PCR. PINK1 mRNA level was normalized to the corresponding GAPDH levels & quantified as a percentage of control (n = 8, t-test). b, c Translation is involved in PINK1 accumulation upon CCCP treatment. HeLa cells were first pre-incubated with 100 μM cycloheximide (CHX) for 2 h & then washed. Cells were further incubated with 10 μM CCCP with or without CHX for 2 h (n = 4, two-way ANOVA). Values are mean ± SEM (n.s. = non-significant, ***p 1000 cells) & are shown as a percentage of control. Values are mean ± SEM (*p < 0.05, **p < 0.01, ***p < 0.001) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27456084), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415483619.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Inhibition of endogenous miR-27a/b function increases human PINK1 expression. a Schematic diagram of sequence alignment of miR-27a/b & anti-miR-27a/b. Asterisks (*) indicate conserved nucleotides. b Inhibition of endogenous miR-27a/b function increased luciferase activities in HeLa cells. Cells were transfected with the reporter constructs containing the full-length 3′UTR of human PINK1 mRNA with wild-type (WT) or mutated (Mut) seed match sites downstream of Renilla luciferase gene. 48 h post-transfection, luciferase activities were measured (n = 4, t-test). c-f Inhibition of endogenous miR-27a/b increased PINK1 protein levels in HeLa (C-D) & M17 cells (E-F). Cells were transfected with 150 nM of anti-miR-27a/b or anti-control (anti-Ctl). 48 h post-transfection, cells were harvested for Western blot. PINK1 protein level was normalized to corresponding GAPDH level & quantified as a percentage of control (n = 4, t-test). Data are shown as a percentage of control. Values are mean ± SEM (n.s. = non-significant, **p < 0.01, ***p < 0.00) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27456084), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482287.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Regulation of PINK1 by miRNA. a Schematic diagram of AGO-specific RNA immunoprecipitation assay. b, cPINK1 mRNAs are associated with miRNA/RISC complex. HeLa cells were transfected with 50 nM of AGO2 siRNA or negative control. 48 h post-transfection, AGO2-bound mRNAs were pulled down from cell lysates with 2A8 anti-AGO2 antibody or non-specific IgG antibody. PINK1 mRNA levels were then measured by qRT-PCR. siRNA against AGO2 served as a quality control for AGO-specific RNA immunoprecipitation assay. PINK1 mRNA levels were quantified as a percentage of group 1 (n = 6, two-way ANOVA). d, e Knock-down of DICER1 increased PINK1 protein levels. HeLa cells were transfected with 50 nM DICER1 siRNA (DICER1 KD) or negative control (Ctl). 48 h post-transfection, cells were harvested for Western blot. The arrowhead indicates a full-length PINK1 band & the asterisk indicates a non-specific band. Each protein level was normalized to corresponding GAPDH level & quantified as a percentage of control (n = 4, t-test). Values are mean ± SEM (n.s. = non-significant, **p < 0.01, ***p < 0.001) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27456084), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482296.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - The expression levels of microtubule protein light chain 3 (LC3B), PTEN inducing putative kinase 1 (PINK1), Parkin, mitofusin 1 (Mfn1), toll-like receptor (TLR) 9, cytochrome c oxidase 4 (COX4), myeloid differentiation factor 88 (MyD88), & nuclear factor (NF)-kappa B in lung tissues from animals with spontaneous breathing (CON) or mechanical ventilation at high tidal volume (HTV) with saline, antimycin A (AmA) or cyclosporine A (CsA). (A) Levels of PINK1, Parkin, & Mfn1 mRNA. (B) Levels of LC3B, PINK1, Parkin, & Mfn1 protein by Western blot. (C) Relative expression of LC3B-II/LC3B-I & PINK1 protein. (D) Relative expression of Parkin & Mfn1 protein. (E) Levels of TLR9 & COX4 mRNA. (F) Levels of MyD88 & nuclear factor-kappa B (NF-kappa B) mRNA. (G) Levels of TLR9, COX4, MyD88, & NF-kappa B protein by Western blot. (H) Relative expression of TLR9 & COX4 protein. (I) Relative expression of MyD88 & NF-kappa B protein. Fold expression for target genes was normalized to that measured for the beta -actin gene. Both of these experiments were in triplicate. aP < 0.05 vs. CON group;bP < 0.05 vs. HTV group; & cP < 0.05 vs. AmA group. Image collected & cropped by CiteAb from the following publication (//www.frontiersin.org/article/10.3389/fimmu.2018.01477/full), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415485118.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Mitophagy contributes to removal of excess mitochondrial fragments in preeclampsia.(a, left panel) Representative TEM image of a cytotrophoblast from PTC & PE placenta collected at 29 weeks. Mitochondrial proximity to ER (MAM) is indicated by white arrows, mitochondrial fission events are depicted by white stars (scale bar: 500 nm; n = 8 separate PE placentae). (a, right panel) percentage of mitochondrial tethering to the ER in in PE vs. PTC (PE placentae, n = 8; PTC placentae, n = 7; unpaired Student’s t-test *P < 0.05). b Representative western blots for MFN2 & calreticulin in ER isolated from PE & PTC placentae (PE & PTC, n = 3 separate samples). c WB & associated densitometry of ASAH2 (normalized to TOM20) in mitochondria from PTC & PE placentae. d Representative TEM depicting mitophagy (white arrow) in cytotrophoblast cell from PE placenta (scale bar: 500 nm, n = 8 separate PE placentae). e Western blot & associated densitometry of PINK1 & Parkin in PE vs. PTC mitochondrial isolates. Densitometry for PINK1 blot was used to calculate the ratio of full-length PINK63kDa to cleaved PINK153kDa (PE & PTC, n = 4 separate placentae, *P < 0.05) Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41419-018-0360-0), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482279.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Deficiency or mutant PINK1 reduces phosphorylation of LETM1 at Thr192. a, b Proteins extracted from PINK1 WT or KO MEFs (a) or mouse brain (b) were subjected to IP with anti-LETM1, probed with pT192 & reprobed with anti-LETM1 by WB. c Proteins extracted from human fibroblast of control (Con) or a PINK1-Q456X patient (Q456X) were subjected to IP with anti-LETM1, probed with pT192 & reprobed with anti-LETM1 by WB. d HEK293 cells were transfected with Adtrack GFP control, AdPINK1-WT, & AdPINK1-Q456X mutant for 1 day. Endogenous LETM1 protein was isolated by IP with anti-LETM1, probed with pT192 & reprobed with anti-LETM1 by WB. e SH-SY5Y cells were treated with 25 µM rotenone for 8 or 16 h. Total cell lysates were either analyzed by WB with anti-PINK1, or subjected to IP with anti-LETM1, probed with pT192 & reprobed with anti-LETM1 antibodies by WB. All above experiments were replicated three times, respectively Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29123128), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482299.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Polyphyllin I suppressed, & PINK1 knockdown further suppressed, tumor growth in a MDA-MB-231 xenograft modelA. Tumor volumes were measured every week & differed at the end of the treatment period (*P < 0.01 compared to shCon cells treated with PPI, ##P< 0.01 compared to shPINK1 cells treated with PPI). B. Representative image of tumors from each group. C. Body weight changes in mice during the 6 weeks of PPI treatment. There were no differences in body weights between the PPI-treated shCon & vehicle-treated shCon groups or between the PPI-treated shPINK1 group & shCon groups. D. Representative tumor tissues were sectioned & subjected to H&E staining, TUNEL assay, & immunohistochemistry staining for C-CASP3. Scale bars: 50 μm. E. Representative tumor tissues from each group were prepared & subjected to western blot using anti-DRP1, -PARK2, -LC3B, -PINK1, & -C-CASP3 antibodies. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.14413), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415483648.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Corticosterone affects NIX-dependent mitophagy through decreasing PGC1 alpha in vivo.a–f Mice exposed to vehicle, corticosterone (10 mg/kg), corticosterone w/ phorbol 12-myristate 13-acetate (PMA pretreatment, 200 μg/kg), or PMA alone for 7 days. a Slide samples for IHC immunostained w/ LAMP1 (green), TOMM20 (red), & DAPI (blue). Scale bars, 100 μm (magnification, ×200). n = 5. b The expressions of NIX, PTEN-induced kinase 1 (PINK1), & BCL2 interacting protein 3 (BNIP3) detected w/ WB where beta -actin used as a loading control. n = 5. c Slide samples for IHC immunostained w/ synpatophysin (green), PSD95 (red), & DAPI (blue). Scale bars, 100 μm (magnification, ×200). n = 5. d Synaptophysin & PSD95 detected by WB. Loading control is beta -actin. n = 5. e The mice subjected to Y-maze test to evaluate spatial memory function. n = 6. f The mice subjected to forced swim test to evaluate depression-like behavior. n = 5. g Vehicle or RU 486 (5 mg/kg) injected mice presented w//w/out corticosterone (10 mg/kg) for 3 days. The expressions of peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC1 alpha ) & NIX visualized via WB. Loading control is beta -actin. n = 5. h The schematic model for mechanisms of inhibition in NIX-dependent mitophagy by glucocorticoid shown. All blots & IF images representative. n = 5 or 6 from each animal w/ two technical replicates each in results of IHC & WB. Quantitative data presented as a mean ± S.E.M. The representative images acquired by SRRF imaging system. Two-sided two-way ANOVA conducted except Fig. 8b, data of which analyzed by two-sided unpaired student’s t test. ** indicates p < 0.01 versus control & ## indicates p < 0.01 versus corticosterone, respectively. Data provided as a Source data file. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33473105), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482218.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - G-TPP activity is conserved in primary fibroblasts(A, C) Fibroblasts were treated with 15 µM G-TPP for the indicated time points. Cells were harvested & western blots were probed with antibodies against (A) PINK1, pS65-Ub & total Ub or (C) autophagy adapter proteins. GAPDH & Vinculin served as loading control. G-TPP treatment led to PINK1 stabilization & pS65-Ub induction in primary skin fibroblasts. p62 levels were induced upon G-TPP treatment, while other adapters seemed decreased. (B, D) Human fibroblasts were treated with 15 µM G-TPP for 16 h & fixed & stained with antibodies against (B) pS65-Ub (green) or (D) the autophagy adapters NBR1, NDP52, p62, OPTN & TAX1BP1 (green). Mitochondria were stained with antibodies against TOM20 (red), nuclei were visualized with Hoechst (blue). Scale bars indicate 10 µM. A magnified image of the boxed region, the fluorescence profile along the arrow & the Pearson’s correlation coefficient of adapter protein & mitochondrial stainingare shown to the right. Shown is the mean ± SEM of at least five randomly selected images (unpaired, two-sided t-test, ***p < 0.0005). Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.22287), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482286.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Polyphyllin I triggers PINK1/PARK2-dependent mitophagyA. MDA-MB-231 cells were treated with 8 μM PPI for different periods of time as indicated, & PARK2, P62, & ubiquitin (UB) levels in mitochondrial fractions were determined by western blot. B. Cells were cotransfected with GFP-UB & RFP-mito & treated with 8 μM PPI for 9 h, after which PARK2 (Alexa Fluor 405, pink) & P62 (Alexa Fluor 647, blue) immunostaining was detected using confocal microscopy. C. Cells cotransfected with GFP-UB & RFP-LC3 were treated with 8 μM PPI for 9 h, after which PARK2 (Alexa Fluor 405, pink) & TOMM20 (Alexa Fluor 647, blue) immunostaining was detected using confocal microscopy. Scale bars: 10 μm. D-E. MDA-MB-231 cells were treated with 8 μM PPI for different periods of time as indicated; whole-cell lysates were then separated on 8% SDS-PAGE gels & analyzed by western blot using the anti-PINK1 antibody. Relative full-length (∼63 kDa) & cleaved (∼52 kDa) PINK1 levels were quantified by densitometry & normalized to Tubulin. The results were expressed as a percentage of control, which was set at 100%. Data are presented as mean ± SD (*P< 0.01 vs. the control). F. Cells were treated with 8 μM PPI for different periods of time as indicated, & whole-cell lysates were then subjected to western blot analysis. G. Cells were treated with 8 μM PPI for 9 h, after which mitochondrial fractions were prepared & subjected to immunoprecipitation using anti-PINK1 antibody; associated PARK2 was detected using immunoblotting. H. RFP-mito-expressing MDA-MB-231 cells were treated with 8 μM PPI for 9 h, & PINK1 (Alexa Fluor 488, green) & PARK2 (Alexa Fluor 405, pink) immunostaining were evaluated using confocal microscopy. Scale bars: 10 μm. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.14413), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482214.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - miR-27a/b suppress human PINK1 expression. a Schematic diagram of the conserved target sites of miR-27a/b in the 3′UTR of human PINK1 mRNA. Seed sequences were indicated in red. Asterisks (*) indicate the conserved nucleotides. b Schematic diagram of the luciferase reporter plasmids. The reporter constructs contain the full-length 3′UTR of human PINK1 mRNA with wild-type (WT) or mutated (Mut) seed match sites downstream of Renilla luciferase gene. c Overexpression of miR-27a/b decreased luciferase activities in HeLa cells. Cells were transfected with miR-27a/b or negative control (Ctl) along with reporter constructs as indicated. 48 h post-transfection, luciferase activities were measured (n = 4, one-way ANOVA). Renilla luciferase activity was normalized to the corresponding firefly luciferase activity. d-g Overexpression of miR-27a/b decreased PINK1 protein levels in HeLa (D-E) & M17 cells (F-G). Cells were transfected with miR-27a/b or negative control (Ctl). 48 h post-transfection, cells were harvested for Western blot (n = 4, t-test). PINK1 protein level was normalized to corresponding GAPDH level & quantified as a percentage of control. Data are shown as a percentage of control. Values are mean ± SEM (n.s. = non-significant, **p < 0.01, ***p < 0.001) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27456084), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415483618.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Increased p62 expression is prevented in PINK1 knock‐down cells. (a) SH‐SY5Y cells expressing scrambled shRNA or PINK1 shRNA (117‐2, 118‐3, & 118‐4) were treated with 10 μM carbonyl cyanide m‐chlorophenylhydrazone (CCCP) for 24 h & full‐length (FL) PINK1 protein levels measured by western blot. No accumulation of FL PINK1 was observed in 118‐3 & 118‐4 PINK1 shRNA clones. (b) SH‐SY5Y cells constitutively expressing scrambled (scram) or PINK1 shRNA (clone 118‐3) were treated with vehicle or 10 μM CCCP for 24 h & p62 protein expression measured by western blotting. **p < 0.05 versus scram CCCP; n = 9. (c) SH‐SY5Y cells were incubated in serum‐free culture media for up to 24 h to induce starvation‐mediated macroautophagy. p62 protein levels were measured by western blotting. *p < 0.05 versus 0 h; **p < 0.01 versus 0 h; n = 4. (d) SH‐SY5Y cells were transfected with scrambled (scram) or p62 siRNA for 72 h. For the last 24 h, cells were treated with vehicle (ethanol) or 10 μM CCCP. p62 protein expression was then measured by western blotting. p62 protein was significantly decreased in p62 siRNA cells under basal conditions & following CCCP treatment, when compared to scram cells. **p < 0.01 versus scram vehicle or scram CCCP; n = 3. (e) Mitochondrial content was measured in SH‐SY5Y cells treated with scram or p62 siRNA for 72 h by measuring citrate synthase (CS) activity. For the last 24 h, cells were treated with vehicle or 10 μM CCCP & data are expressed as % of vehicle. *p < 0.05 versus scram CCCP treatment; n = 5. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26509433), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482278.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - NF kappa B upregulates human PINK1 gene expression. (A) NF kappa B increases the endogenous human PINK1 mRNA level. HEK293 cells were transfected with either the NF kappa B expression vector or empty vector pMTF. RT-PCRs were performed using either primers specific to the human PINK1 coding sequence or the human beta -actin coding sequence. (B) NF kappa B increases the endogenous human PINK1 protein levels. HEK293 cells transfected with NF kappa B were harvested 48 h after transfection for protein detection. Cell lysates were run on 10% glycine gel & images were collected by Licor. A significant increase of endogenous PINK1 was observed. (C) The endogenous human PINK1 protein level was dramatically increased by NF kappa B in SH-SY5Y cells. SH-SY5Y cells were transfected with NF kappa B p65 plasmids or the control vector pMTF & then harvested for protein detections. The human PINK1 protein & its proteolysis products ∆1-PINK1 (55kD) & ∆2-PINK1 (45kD) were all increased. beta -actin acted as the internal control. (D) LPS treatment facilitated PINK1 expression in SH-SY5Y cells. Cells were harvested after being treated for 16 h & then subjected to Western blot. The human beta -actin level was served as a control. Quantification was performed by Image J software. Values indicate means ± SEM. n = 3, *p <0.01 by Student’s t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25108683), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415485116.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - G-TPP induces PINK1 stabilization & kinase activity in HeLa cells(A) G-TPP treatment leads to PINK1 stabilization & pS65-Ub induction in HeLa cells. HeLa cells stably expressing untagged Parkin were treated with 10 µM G-TPP for the indicated times. Western blots were prepared with cell lysates & probed with antibodies against PINK1 & pS65-Ub. GAPDH served as a loading control. (B) pS65-Ub is induced in G-TPP treated cells & co-localizes with EGFP-Parkin & mitochondria. HeLa cells stably expressing EGFP-Parkin (green) were treated with 10 µM G-TPP for the indicated times & fixed. Cells were stained with antibodies against pS65-Ub (red) & the mitochondrial marker TOM20 (cyan). Scale bars correspond to 10 µM. (C) Quantification of Parkin translocation using High Content Imaging. HeLa EGFP-Parkin cells were treated for 4 or 8 h with or without 10 µM G-TPP. CCCP treatment (10 µM for 2 h) was used as a positive control. Cells were fixed, counterstained with Hoechst dye to visualize nuclei, imaged & analyzed using the ratio of cytoplasmic to nuclear EGFP signal [21]. Data was normalized to positive (2 h 10 µM CCCP treatment) & negative (2 h DMSO) controls. G-TPP significantly induced Parkin re-localization to levels similar to or beyond 2 h CCCP treatment. Shown are the mean values of three independent experiments with triplicate wells each ± SEM (one-way ANOVA with Tukey’s posthoc, ***p < 0.0005). Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.22287), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-31020241548369.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - NF kappa B upregulates human PINK1 gene expression. (A) NF kappa B increases the endogenous human PINK1 mRNA level. HEK293 cells were transfected with either the NF kappa B expression vector or empty vector pMTF. RT-PCRs were performed using either primers specific to the human PINK1 coding sequence or the human beta -actin coding sequence. (B) NF kappa B increases the endogenous human PINK1 protein levels. HEK293 cells transfected with NF kappa B were harvested 48 h after transfection for protein detection. Cell lysates were run on 10% glycine gel & images were collected by Licor. A significant increase of endogenous PINK1 was observed. (C) The endogenous human PINK1 protein level was dramatically increased by NF kappa B in SH-SY5Y cells. SH-SY5Y cells were transfected with NF kappa B p65 plasmids or the control vector pMTF & then harvested for protein detections. The human PINK1 protein & its proteolysis products ∆1-PINK1 (55kD) & ∆2-PINK1 (45kD) were all increased. beta -actin acted as the internal control. (D) LPS treatment facilitated PINK1 expression in SH-SY5Y cells. Cells were harvested after being treated for 16 h & then subjected to Western blot. The human beta -actin level was served as a control. Quantification was performed by Image J software. Values indicate means ± SEM. n = 3, *p <0.01 by Student’s t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25108683), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482277.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - NF kappa B upregulates human PINK1 gene expression. (A) NF kappa B increases the endogenous human PINK1 mRNA level. HEK293 cells were transfected with either the NF kappa B expression vector or empty vector pMTF. RT-PCRs were performed using either primers specific to the human PINK1 coding sequence or the human beta -actin coding sequence. (B) NF kappa B increases the endogenous human PINK1 protein levels. HEK293 cells transfected with NF kappa B were harvested 48 h after transfection for protein detection. Cell lysates were run on 10% glycine gel & images were collected by Licor. A significant increase of endogenous PINK1 was observed. (C) The endogenous human PINK1 protein level was dramatically increased by NF kappa B in SH-SY5Y cells. SH-SY5Y cells were transfected with NF kappa B p65 plasmids or the control vector pMTF & then harvested for protein detections. The human PINK1 protein & its proteolysis products ∆1-PINK1 (55kD) & ∆2-PINK1 (45kD) were all increased. beta -actin acted as the internal control. (D) LPS treatment facilitated PINK1 expression in SH-SY5Y cells. Cells were harvested after being treated for 16 h & then subjected to Western blot. The human beta -actin level was served as a control. Quantification was performed by Image J software. Values indicate means ± SEM. n = 3, *p <0.01 by Student’s t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25108683), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-31020241548363.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - G-TPP leads to recruitment of autophagy adapters & degradation of mitochondria(A) HeLa cells stably expressing untagged Parkin were treated with 10 µM G-TPP for 8 h. Western blots were prepared from cell lysates & probed with antibodies against LC3, phospho-TBK1 (Ser172) & TBK1. GAPDH was used as a loading control. Upon 8 h the levels of LC3-I & LC3-II were both increased. At 8 h after treatment with G-TPP but not at 4 or 24 h, TBK1 was phosphorylated. (B) HeLa cells stably expressing EGFP-Parkin were treated with 10 µM G-TPP & fixed 8 h after treatment. Cells were stained with antibodies against the autophagy adapter proteins NBR1, NDP52, OPTN, p62, & TAX1BP1 (red). Mitochondria were counterstained with TOM20 antibodies (cyan), nuclei with Hoechst (blue). EGFP-Parkin epifluorescence is shown in green. Scale bar corresponds to 10 µM. (C) HeLa cells stably expressing EGFP-Parkin & the reporter protein mitoKeima were treated with 10 µM CCCP or G-TPP & imaged over time. The ratio of ‘neutral’ mitoKeima to ‘acidic’ mitoKeima was calculated as readout for mitophagy. Parkin translocation was monitored at the same time. Values for Parkin translocation & mitophagy were normalized to 12 h treatment with 10 µM CCCP as positive control & DMSO as negative control (two-way ANOVA with Tukey’s post-hoc test, **p < 0.005, ***p < 0.0005). Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.22287), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482225.jpg)
![Western Blot: Rabbit Polyclonal PINK1 Antibody [BC100-494] - PINK1 detection in mouse and postmortem human cortex samples. 1:1000 dilution at 4 degrees overnight to detect endogenous PINK1 from mouse and postmortem human cortex samples (10 ug total protein). Image from a verified customer review.](http://images.novusbio.com/fullsize/antibody/bc100-494_rabbit-polyclonal-pink1-antibody-western-blot-231202510057..jpg)
![Western Blot: Carbonic Anhydrase IX/CA9 Antibody - BSA Free [NB100-417] - Analysis of protein levels of genes with increased transcription in hypoxia, IOX2 & VH032.HIF targets were increased in hypoxia, VH298 & FG-4592. 0.05% DMSO (vehicle control), 1% O2 (hypoxia), 100 µM VH298 & 50 µM FG-4592 were introduced to (A) HeLa or HFF for 24 hours & (B) HeLa for indicated time. Protein levels were analysed by immunoblotting using antibodies against indicated proteins, with beta -Actin as loading control. The blots shown are representative of three independent experiments. * indicates longer exposure. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30801039), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-417_rabbit-polyclonal-carbonic-anhydrase-ix-ca9-antibody-310202415394513.jpg)
![Immunohistochemistry-Paraffin: Carbonic Anhydrase IX/CA9 Antibody - BSA Free [NB100-417] - IGF1R & CA9 expression in PDAC.(A) Representative staining of CA9 cells quantified on a scoring system of 0–3 according to staining intensity (original magnification ×200). CA9 was mainly expressed in the cell membrane of PDAC cells. (B) IGF1R was mainly expressed in the cytoplasm of PDAC cells. (C) Association between IGF1Rexpression & CA9 expression in 120 pancreas cancer. A significant correlation was found between IGF1R expression level was significantly correlated with CA9 expression in PDAC cells (p < 0.01, rs = 0.649; Spearman’s rank sum test). The size of circle indicates the number of PDAC patients. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27487118), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-417_rabbit-polyclonal-carbonic-anhydrase-ix-ca9-antibody-310202415382445.jpg)
![Immunohistochemistry: Carbonic Anhydrase IX/CA9 Antibody - BSA Free [NB100-417] - Representative human colorectal cancer specimen. Immunohistochemistry of CA9 & GGT1 in mLNs. In these cases, both CA9 & GGT1 were expressed, suggesting that GGT1 expression is related to hypoxia in mLNs. Scale bar, 500 μm. Black arrowheads: GGT of cancer cells, white arrowheads: GGT surrounding cancer cells, arrow: accumulation of GGT. mLNs: metastatic lymph nodes, GGT: gamma-glutamyl transpeptidase. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30542087), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-417_rabbit-polyclonal-carbonic-anhydrase-ix-ca9-antibody-310202415293313.jpg)
![Immunohistochemistry: Carbonic Anhydrase IX/CA9 Antibody - BSA Free [NB100-417] - Representative microscopy images of staining for hypoxia markers in prostate tissues (MO, 400×). A) HIF-1 alpha - notice the granular cytoplasmic immunoreactivity of the malignant epithelial cells. In this case, more than 50% of the glands stained. B) LOX - strong & diffuse nuclear immunoreactivity of the epithelial cells. C) CAIX - note a focal apical cytoplasmic immunoreactivity in epithelial cells. D) VEGFR2 - moderate nuclear & weak cytoplasmic expression of the epithelial cells Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28143503), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-417_rabbit-polyclonal-carbonic-anhydrase-ix-ca9-antibody-310202415171346.jpg)
![Immunohistochemistry: Carbonic Anhydrase IX/CA9 Antibody - BSA Free [NB100-417] - The images are representative of immunohistochemistry staining of nuclear staining of proliferation marker Ki67, membrane protein CD 44, & CA IX. The images of scaffold culture (left panel) are compared with cell pellet paraffin section (right panel). The scaffold dissolved in xylene presented as a clear region marked ∗. All scale bars are 100 μm, magnification 40x. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24101930), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-417_rabbit-polyclonal-carbonic-anhydrase-ix-ca9-antibody-310202415371932.jpg)
![Immunohistochemistry: Carbonic Anhydrase IX/CA9 Antibody - BSA Free [NB100-417] - Hypoxia, blood vessel & proliferation staining. IHC staining in the Biopsy 23 & Biopsy 3 respectively for CA-9, EF5, CD31, Ki67 & LYVE1. 15× Magnification. Image collected & cropped by CiteAb from the following publication (//www.mdpi.com/2072-6694/4/3/821), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-417_rabbit-polyclonal-carbonic-anhydrase-ix-ca9-antibody-310202415304258.jpg)
![Western Blot: Carbonic Anhydrase IX/CA9 Antibody - BSA Free [NB100-417] - VH298 elicits a HIF-dependent hypoxic response in various cell lines.1% DMSO, hypoxia (1% O2) & indicated compounds at 100 μM were introduced to (a) HFF, HeLa, U2OS & (b) RCC4 cells expressing HA-tagged VHL (with the exception of cis-VH298 & VH298 used at 150 μM) for 24 h & (c) CTLs for 8 h. Protein levels were analysed by immunoblotting using antibodies against the indicated proteins, with beta -actin (SMC1 for CTLs) as the loading control. The blots shown are representative of three independent experiments. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27811928), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-417_rabbit-polyclonal-carbonic-anhydrase-ix-ca9-antibody-31020241535610.jpg)
![Immunohistochemistry: Carbonic Anhydrase IX/CA9 Antibody - BSA Free [NB100-417] - HE staining & immunohistochemistry (CA9 & GGT1) of fixed primary tumor & mLN specimens from orthotopic mouse model. CA9 & GGT1 were expressed inside the primary tumor & in mLNs. GGT1 was accumulated in the area of central necrosis. HE: hematoxylin-eosin. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30542087), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-417_rabbit-polyclonal-carbonic-anhydrase-ix-ca9-antibody-31020241529339.jpg)
![Western Blot: Carbonic Anhydrase IX/CA9 Antibody - BSA Free [NB100-417] - Analysis of protein levels of genes with increased transcription in hypoxia, IOX2 & VH032.HIF targets were increased in hypoxia, VH298 & FG-4592. 0.05% DMSO (vehicle control), 1% O2 (hypoxia), 100 µM VH298 & 50 µM FG-4592 were introduced to (A) HeLa or HFF for 24 hours & (B) HeLa for indicated time. Protein levels were analysed by immunoblotting using antibodies against indicated proteins, with beta -Actin as loading control. The blots shown are representative of three independent experiments. * indicates longer exposure. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30801039), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-417_rabbit-polyclonal-carbonic-anhydrase-ix-ca9-antibody-31020241535621.jpg)
![Immunohistochemistry: Carbonic Anhydrase IX/CA9 Antibody - BSA Free [NB100-417] - Comparison between primary tumor & mLNs of the mouse model. Expression of CA9 & GGT1 in mLNs was higher than that in the primary tumor at 1week after injection of cells. (A) CA9 & GGT1 expression of HT29 mLNs compared to primary tumor at 6 weeks or 1 week after injection of cells. (B) Tissue oxygen concentration (%) of rectal submucosa (SM) & nLNs (n = 3). Error bars represent SD. mNs: metastatic lymph nodes, nLNs: non metastatic lymph nodes. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30542087), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-417_rabbit-polyclonal-carbonic-anhydrase-ix-ca9-antibody-310202415392514.jpg)
![Immunohistochemistry: Carbonic Anhydrase IX/CA9 Antibody - BSA Free [NB100-417] - Chemosensitivity of the CTC SCLC lines (IC50, mean ± SD) & immunohistochemistry of sections of tumorospheres. All differences between single cells (SC) & tumorospheres (TS) are statistically significant. Immunohistochemical staining of sections of UHGc5, BHGc16 & BHGc26 CTCs was performed using antibodies directed to CD56, CHGA, CAIX & Ki67, respectively. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-05562-z), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-417_rabbit-polyclonal-carbonic-anhydrase-ix-ca9-antibody-310202415394539.jpg)
![Western Blot: Carbonic Anhydrase IX/CA9 Antibody - BSA Free [NB100-417] - Analysis of protein levels of genes with increased transcription in hypoxia, IOX2 & VH032.HIF targets were increased in hypoxia, VH298 & FG-4592. 0.05% DMSO (vehicle control), 1% O2 (hypoxia), 100 µM VH298 & 50 µM FG-4592 were introduced to (A) HeLa or HFF for 24 hours & (B) HeLa for indicated time. Protein levels were analysed by immunoblotting using antibodies against indicated proteins, with beta -Actin as loading control. The blots shown are representative of three independent experiments. * indicates longer exposure. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30801039), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-417_rabbit-polyclonal-carbonic-anhydrase-ix-ca9-antibody-31020241539596.jpg)
![Immunocytochemistry/ Immunofluorescence: Carbonic Anhydrase IX/CA9 Antibody - BSA Free [NB100-417] - Immunocytochemical analysis of CNHCs with antibodies against the RCC marker CAIX. Clusters of CNHCs cytomorphologically classified as uncertain malignant (−UMF) with cytoplasmic positive staining with antibodies against the RCC marker CAIX (A). Clusters of CNHC-UMF & -BF without reactivity for CAIX antibodies (B & C, respectively). A single CNHC-MF with positive cytoplasmic (D) & without staining for CAIX (E). Single CAIX-negative CNHC-UMF & -BF (F & G, respectively). Image collected & cropped by CiteAb from the following publication (//translational-medicine.biomedcentral.com/articles/10.1186/1479-5876-11-214), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-417_rabbit-polyclonal-carbonic-anhydrase-ix-ca9-antibody-310202415171339.jpg)
![Western Blot: Carbonic Anhydrase IX/CA9 Antibody - BSA Free [NB100-417] - GPRC5A promotes hypoxic cell survival via YAPAHypoxia induced increased total YAP expression in a panel of colorectal cancer cell lines. Actin confirmed equal loading; blots are representative of at least two independent experiments. Related to Fig 4.B–EqRT–PCR analysis revealed that hypoxia increased the expression of known YAP target genes AREG, BCL2L1 (BCL‐XL), CTGF & CYR61. Representative experiments are shown. Representative examples of n = 3 independent experiments are shown; data are presented as mean ± SD.FIncreased expression of YAP Ser397 in GPRC5A‐depleted cells was overridden by expression of constitutively active RhoA (G14V) in hypoxia. Expression of dominant negative RhoA (T19N) did not further increase YAP Ser397 phosphorylation in response to GPRC5A depletion.GDarker exposure of the GPRC5A blot in Fig 4I, confirming expression of 30–40 kDa & 80 kDa species. Note that YAP siRNA partially diminishes GPRC5A in line with the existence of positive HIF‐GPRC5A‐YAP feedback loop. Asterisk (*) indicates non‐specific band.Source data are available online for this figure. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30143543), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-417_rabbit-polyclonal-carbonic-anhydrase-ix-ca9-antibody-31020241612652.jpg)
![Immunohistochemistry: Carbonic Anhydrase IX/CA9 Antibody - BSA Free [NB100-417] - CAIX expression in PDAC & association with outcomeA. Representative images of immunohistochemical staining showing: negative expression of CAIX in both tumor cell & stromal compartments (top left), positive expression of CAIX in tumor cells but not stromal compartment (top right), positive expression of CAIX in stromal compartment but not tumor cells (bottom left), positive expression of CAIX in both tumor cell & stromal compartments (bottom right). B. Kaplan-Meier analysis of CAIX expression in the distinct tumor cell & stromal compartments & the associated overall survival. C. Representative images of immunohistochemical staining showing low stromal volume & high stromal volume & low & high microvessel density D. Representative images of immunohistochemical staining showing: positive expression of MCT4 in tumor cell compartment & positive expression of MCT4 in tumor stromal compartment. Kaplan-Meier analysis of combinatorial MCT4 & CAIX expression in the stromal compartment & the associated overall survival. Hazard ratios & p-values for each comparison are summarized in the table. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27623078), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-417_rabbit-polyclonal-carbonic-anhydrase-ix-ca9-antibody-310202415535129.jpg)
![Immunocytochemistry/ Immunofluorescence: Carbonic Anhydrase IX/CA9 Antibody - BSA Free [NB100-417] - Hypoxia & autophagy markers in breast cancer stem-cells(A) Co-expression of CD133 & BECLIN1 in pCR & non-pCR patients. Double IF X800. (B) Tumor cells (T) distributed around necrosis (N) express LC3B with typical cytoplasmic punctuated staining, ×1000. Double IF shows that some CD133-positive tumor cells co-express LC3B. ×400. (C) Tumor cells (T) distributed around necrosis (N) express CAIX, on their cytoplasmic membrane, ×1000. Double IF shows a co-expression of LC3B & CAIX in some tumor cells. ×400. (D) Laser microdissection of CD133-positive cells. (E) Laser-microdissected CD133-positive cells express PROMININ & not PTPRC (CD45). (F) mRNA relative quantification of HIF1A, CAIX, LC3B, BECN1, & BNIP3L show a significantly higher expression level in CD133-positive cells versus CD133-negative cells, in the 35 non-pCR biopsies. *p < 0.05. (G) Multivariate analysis of tumor cell characteristics & pCR shows an inverse correlation between pCR & cells bearing markers of stemness or autophagy. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28445132), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-417_rabbit-polyclonal-carbonic-anhydrase-ix-ca9-antibody-310202415525275.jpg)
![Immunocytochemistry/ Immunofluorescence: Carbonic Anhydrase IX/CA9 Antibody - BSA Free [NB100-417] - Immunofluorescent images showing CAIX expression, pimonidazole, apoptosis & proliferation in SCCNij202.CAIX is expressed in hypoxic regions as assessed by pimonidazole staining (A), but is also observed in non-pimonidazole areas (B). Yet, most of CAIX is expressed in pimonidazole positive regions (C). Proliferation (BrdUrd) & apoptosis (caspase-3) in relation to CAIX expression are shown in figure D & E respectively. Red, CAIX; Green, pimonidazole (A–B), BrdUrd (D) or caspase-3 (E); Yellow, overlap of CAIX (red) & pimonidazole (green); Light blue, vessels. Magnification 100×. Scale bars represent 100 µm. Closed circles represent CAIX expression in pimonidazole positive regions; open circles represent CAIX expression in pimonidazole negative regions. Abbrevations: 1× S4, 8 h, one i.p. injection S4, harvest after 8 hours; 1× S4, 24 h, one i.p. injection S4, harvest after 24 hours; 3× S4, one i.p. injection S4 a day for 3 days, harvest 8 hours after the last injection; 5× S4, one i.p. injection S4 a day for 5 days, harvest 8 hours after the last injection. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25225880), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-417_rabbit-polyclonal-carbonic-anhydrase-ix-ca9-antibody-31020241554518.jpg)
![Immunohistochemistry: Carbonic Anhydrase IX/CA9 Antibody - BSA Free [NB100-417] - Colorectal cancer xenograft growth was suppressed by CB-PIC(20 & 50 mg/kg body weight) in female athymic nude mice. Starting three days after SW620 cell inoculation, CB-PIC (20 & 50 mg/kg body weight) was injected in abdomen with 4% Tween 20 as vehicle once daily. (a) Body weights of mice. (b) Tumor growth in a time course. (c) Final tumor weight at termination of experiment. (d) Representative examples of immunohistochemical staining for Ki-67, CD34, TUNEL, CA IX & pAMPK alpha in tumor sections. Graphs show the Ki67 index (proliferation), CD34 index (angiogenesis), TUNEL index (apoptosis), CA IX (hypoxia region), & pAMPK alpha index in tumor sections. Values are means ± SD, n = 6. *P < 0.05 & ***P < 0.001 compared with control mice. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23589723), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-417_rabbit-polyclonal-carbonic-anhydrase-ix-ca9-antibody-310202415525266.jpg)
![Western Blot: Carbonic Anhydrase IX/CA9 Antibody - BSA Free [NB100-417] - Hypoxia induces GPRC5A directly via HIFsASILAC‐based proteomics data identify known (red) & novel (green) hypoxia‐induced proteins in SW620 cells. One‐sample t‐test was performed.BWestern blotting confirmed GPRC5A as a hypoxia‐induced protein in SILAC lysates.CValidation of GPRC5A Western blot data using siRNA. *Non‐specific band of ˜60 kDa not depleted by GPRC5A siRNA.DConfocal microscopy showing plasma membrane GPRC5A expression in hypoxic SW620 cells (scale bars: 75 μm).EWestern blotting showing GPRC5A upregulation by hypoxia in a panel of colorectal tumour cell lines.FBasal & hypoxia‐induced GPRC5A protein expression was decreased by HIF‐1/2 alpha depletion.GDepletion of HIF‐1 beta decreased GPRC5A protein upregulation in hypoxia.HHypoxia mimetic DMOG induced HIF‐1/2 alpha , CA9 & GPRC5A protein expression. Dual HIF‐1/2 alpha depletion reduced GPRC5A induction by DMOG.IqRT–PCR demonstrating that GPRC5A mRNA was upregulated by hypoxia (n = 3). GPRC5A was normalised to HPRT (error bars ± SD).JqRT–PCR demonstrating that HIF‐1/2 alpha depletion decreased GPRC5A induction during hypoxia (n = 3). GPRC5A was normalised to HPRT (error bars ± SD).KChIP‐PCR analyses identify HIF‐1 alpha binding to the GPRC5A promoter region containing a putative optimal HRE (error bars ± SD, n = 3).Data information: Asterisks (*) indicate non‐specific band. Level adjustments were made to images in Adobe Photoshop post‐acquisition for clarity (equal changes applied to the entire image). Representative examples of n = 3 independent experiments are shown.Source data are available online for this figure. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30143543), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-417_rabbit-polyclonal-carbonic-anhydrase-ix-ca9-antibody-310202415535151.jpg)
![Immunocytochemistry/ Immunofluorescence: Carbonic Anhydrase IX/CA9 Antibody - BSA Free [NB100-417] - Immunofluorescent images showing CAIX expression, pimonidazole, apoptosis & proliferation in SCCNij202.CAIX is expressed in hypoxic regions as assessed by pimonidazole staining (A), but is also observed in non-pimonidazole areas (B). Yet, most of CAIX is expressed in pimonidazole positive regions (C). Proliferation (BrdUrd) & apoptosis (caspase-3) in relation to CAIX expression are shown in figure D & E respectively. Red, CAIX; Green, pimonidazole (A–B), BrdUrd (D) or caspase-3 (E); Yellow, overlap of CAIX (red) & pimonidazole (green); Light blue, vessels. Magnification 100×. Scale bars represent 100 µm. Closed circles represent CAIX expression in pimonidazole positive regions; open circles represent CAIX expression in pimonidazole negative regions. Abbrevations: 1× S4, 8 h, one i.p. injection S4, harvest after 8 hours; 1× S4, 24 h, one i.p. injection S4, harvest after 24 hours; 3× S4, one i.p. injection S4 a day for 3 days, harvest 8 hours after the last injection; 5× S4, one i.p. injection S4 a day for 5 days, harvest 8 hours after the last injection. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25225880), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-417_rabbit-polyclonal-carbonic-anhydrase-ix-ca9-antibody-310202415525233.jpg)
![Immunocytochemistry/ Immunofluorescence: Carbonic Anhydrase IX/CA9 Antibody - BSA Free [NB100-417] - Immunofluorescent images showing CAIX expression, pimonidazole, apoptosis & proliferation in SCCNij202.CAIX is expressed in hypoxic regions as assessed by pimonidazole staining (A), but is also observed in non-pimonidazole areas (B). Yet, most of CAIX is expressed in pimonidazole positive regions (C). Proliferation (BrdUrd) & apoptosis (caspase-3) in relation to CAIX expression are shown in figure D & E respectively. Red, CAIX; Green, pimonidazole (A–B), BrdUrd (D) or caspase-3 (E); Yellow, overlap of CAIX (red) & pimonidazole (green); Light blue, vessels. Magnification 100×. Scale bars represent 100 µm. Closed circles represent CAIX expression in pimonidazole positive regions; open circles represent CAIX expression in pimonidazole negative regions. Abbrevations: 1× S4, 8 h, one i.p. injection S4, harvest after 8 hours; 1× S4, 24 h, one i.p. injection S4, harvest after 24 hours; 3× S4, one i.p. injection S4 a day for 3 days, harvest 8 hours after the last injection; 5× S4, one i.p. injection S4 a day for 5 days, harvest 8 hours after the last injection. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25225880), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-417_rabbit-polyclonal-carbonic-anhydrase-ix-ca9-antibody-31020241683941.jpg)
![Western Blot: Carbonic Anhydrase IX/CA9 Antibody - BSA Free [NB100-417] - Establishment of a human protein replacement stable cell line using 47snoMEN.(a) Images of protein replacement stable cell lines (U2OSGFP–HIF-1 alpha -47PR). Expression of FP proteins was confirmed by fluorescence imaging with DFX treatment. Bar is 10 μm. (b) U2OS & U2OSGFP–HIF-1 alpha -47PR cells were exposed to 1% O2 for the indicated periods of time prior to lysis. Cell extracts were analysed by western blot using the indicated antibodies. (c) U2OS cells were transfected with 1 μg of control & HIF-1 alpha -47snoMEN vectors for 48 hours prior to lysis. DFX was added for the last 24 hours. Cell extracts were analysed by western blot using the indicated antibodies. (d) 3D culture analysis. HeLaGFP–HIF-1 alpha -47PR cells were cultured in lipidure coated plates to induce spheroid formation. HIF-1 alpha is visible in the core of the spheroid revealing hypoxia. Bar is 10 μm. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0154759), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-417_rabbit-polyclonal-carbonic-anhydrase-ix-ca9-antibody-310202415541935.jpg)
![Immunocytochemistry/ Immunofluorescence: Carbonic Anhydrase IX/CA9 Antibody - BSA Free [NB100-417] - Immunofluorescent images showing CAIX expression, pimonidazole, apoptosis & proliferation in SCCNij202.CAIX is expressed in hypoxic regions as assessed by pimonidazole staining (A), but is also observed in non-pimonidazole areas (B). Yet, most of CAIX is expressed in pimonidazole positive regions (C). Proliferation (BrdUrd) & apoptosis (caspase-3) in relation to CAIX expression are shown in figure D & E respectively. Red, CAIX; Green, pimonidazole (A–B), BrdUrd (D) or caspase-3 (E); Yellow, overlap of CAIX (red) & pimonidazole (green); Light blue, vessels. Magnification 100×. Scale bars represent 100 µm. Closed circles represent CAIX expression in pimonidazole positive regions; open circles represent CAIX expression in pimonidazole negative regions. Abbrevations: 1× S4, 8 h, one i.p. injection S4, harvest after 8 hours; 1× S4, 24 h, one i.p. injection S4, harvest after 24 hours; 3× S4, one i.p. injection S4 a day for 3 days, harvest 8 hours after the last injection; 5× S4, one i.p. injection S4 a day for 5 days, harvest 8 hours after the last injection. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25225880), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-417_rabbit-polyclonal-carbonic-anhydrase-ix-ca9-antibody-31020241612665.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 01. Liver Hepatocellular Carcinoma](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0060.jpg "Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 01. Liver Hepatocellular Carcinoma")
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - Human Liver Tissue Microarray (Cancer metastasis) [NBP2-30221] - 02. Hepatocellular carcinoma](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0061.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - Liver Hepatocellular carcinoma](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0062.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 04. Liver Hepatocellular Carcinoma](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0063.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - Liver Combined Hepatocellular carcinoma](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0064.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - Liver Hepatocwellular Carcinoma](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0065.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 07. Liver Hepatocellular carcinoma](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0066.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 08. Liver hepatocellular carcinoma Well differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0067.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 09. Liver hepatocellular carcinoma Well differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0068.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 10. liver hepatocellular carcinoma Well differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0069.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 11. Liver hepatocellular carcinoma moderately differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0070.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 12. Liver Hepatocellular Carcinoma Moderately Differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0071.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 13. Liver hepatocellular carcinoma well differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0072.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 14. Liver hepatocellular carcinoma moderately differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0073.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 15. Liver hepatocellular carcinoma](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0074.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 16. Liver hepatocellular carcinoma, moderately differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0075.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 17. Liver hepatocellular carcinoma, moderately differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0076.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 18. Liver hepatocellular carcinoma, Poorly differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0077.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 19. Liver hepatocellular carcinoma, Well differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0078.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 20. Liver hepatocellular carcinoma, Poorly differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0079.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 21. Liver hepatocellular carcinoma, Moderately differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0080.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 22. Liver hepatocellular carcinoma, Moderately differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0081.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 23. Liver hepatocellular carcinoma, Moderately differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0082.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 24. Liver hepatocellular carcinoma, Moderately differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0083.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 25. Liver hepatocellular carcinoma, Well differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0084.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 26. Liver hepatocellular carcinoma, Moderately differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0085.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 27. Liver hepatocellular carcinoma, Poorly differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0086.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 28. Liver hepatocellular carcinoma, Moderately differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0087.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 29. Liver hepatocellular carcinoma, Poorly differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0088.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 30. Liver hepatocellular carcinoma, Moderately differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0089.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 31. Liver hepatocellular carcinoma, Moderately differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0090.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 32. Liver hepatocellular carcinoma, Moderately differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0091.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 33. Liver hepatocellular carcinoma, Well differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0092.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 34. Liver hepatocellular carcinoma, Moderately differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0093.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 35. Liver hepatocellular carcinoma](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0094.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 36. Liver hepatocellular carcinoma, Moderately differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0095.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 37. Liver hepatocellular carcinoma, Moderately differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0096.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 38. Liver hepatocellular carcinoma, Moderately differentiated](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0097.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 39. Liver cholangiocarcinoma](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0098.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 40. Liver cholangiocarcinoma](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0099.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 41. Colon metastatic heptocellular carcinoma](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0100.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 42. Lung metastatic hepatocellular carcinoma](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0101.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 43. Liver: cancer-metastasis-normal](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0103.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 44. adrenal gland metastatic hepatocellular Carcinoma](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0104.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 45. Lumbar Vertebra metastatic hepatocellular carcinoma](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0105.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 46. Colon metastatic hepatocellular carcinoma](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0106.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 47. Soft Tissue metastatic hepatocellular Carcinoma](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0107.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 48. Lymph node, metastatic hepatocellular carcinoma](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0108.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 49. Soft Tissue, metastatic Chloangiocarcinoma](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0109.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 50. Lymph node, Metastatic Cholangiocarcinoma](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0110.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 51. Liver (adjacent to cancer)](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0111.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 52. Liver (adjacent to cancer)](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0112.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 53. Liver (adjacent to cancer)](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0113.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 54. Liver (adjacent to cancer)](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0114.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 55. Liver, adjacent to cancer](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0115.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 56. Liver, non-neoplastic liver (apart from cancer, match of #5)](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0116.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 57. Liver (apart from cancer)](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0117.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 59. Liver (apart from cancer)](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0118.jpg)
![Hematoxylin & Eosin Stain: Human Liver Tissue MicroArray (Cancer metastasis) [NBP2-30221] - 58. Liver apart from cancer](http://images.novusbio.com/fullsize/Human-Liver-Tissue-MicroArray-Cancer-metastasis-Hematoxylin-&-Eosin-Stain-NBP2-30221-img0119.jpg)
![Hematoxylin & Eosin Stain: Liver Matched Tumor & Normal Tissue Slides (Tumor) [NBP2-77672] - Tissue: Human Liver Tumor, Pathology: Primary Tumor](http://images.novusbio.com/fullsize/Liver-Matched-Tumor-&-Normal-Tissue-Slides-Tumor-Hematoxylin-&-Eosin-Stain-NBP2-77672-img0002.jpg "Hematoxylin & Eosin Stain: Liver Matched Tumor & Normal Tissue Slides (Tumor) [NBP2-77672] - Tissue: Human Liver Tumor, Pathology: Primary Tumor")
![Hematoxylin & Eosin Stain: Liver Matched Tumor & Normal Tissue Slides (Tumor) [NBP2-77672] - Tissue: Human Liver, Pathology: Adjacent normal tissue](http://images.novusbio.com/fullsize/Liver-Matched-Tumor-&-Normal-Tissue-Slides-Tumor-Hematoxylin-&-Eosin-Stain-NBP2-77672-img0001.jpg)