| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB110-67828 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-2331SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB110-89474SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Purified | NBP3-25349-0.025mg | |||
| Purified | NBP3-25349-0.05mg | |||
| BSA Free | NB100-142SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP3-38565-20ul | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP1-88269-25ul | |||
HAF017). Specific bands were detected for TrkB at approximately 95 kDa and 145 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." alt="Western blot shows lysates of human brain (motor cortex) tissue, mouse brain (cortex) tissue, and rat brain (hippocampus) tissue. PVDF membrane was probed with 0.1 µg/mL of Goat Anti-Human/Mouse/Rat TrkB Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1494) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (HAF017). Specific bands were detected for TrkB at approximately 95 kDa and 145 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." class="big_thumb" />
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Carrier Free | AF1494-SP | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP2-00362-500ug | |||
| BSA Free | NBP2-00362-0.025mg | |||
![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] - 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)
![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)
![Western Blot: Mouse Monoclonal beta-Actin Antibody (AC-15) [NB600-501] - Quantification of TNF alpha in bone graft in the tibia of intrailiac cellularized goats at different times compared with tibial autograft and untreated bone defect. Beta-actin antibody (Catalog # NB600-501) was used at a dilution of 1:3000 and TNF alpha antibody (Catalog # NBP1-97453) was used at a dilution of 1:1000. Evaluation of pre-cellularized graft in iliac crest in the treatment of bone defects in the tibia of goats. G1: cellularized graft for 4 weeks applied to tibial bone defect, G2: cellularized graft for 6 weeks applied to tibial bone defect, G3: cellularized graft for 8 weeks applied to tibial bone defect, G4: tibial autograft and G5: untreated bone defect. All groups were evaluated 10 days after graft implantation. Image from a verified customer review.](http://images.novusbio.com/fullsize/antibody/nb600-501_mouse-monoclonal-beta-actin-antibody-ac-15-western-blot-295202514159..jpg)
![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] - 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)
![<b>Biological Strategies Validation. </b>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] - 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)
![Simple Western: ACE-2 Antibody [Unconjugated] [AF933] - Design for a membrane-localized ACE2 expression system. (A) Our ACE2 construct is driven by a CMV promoter followed by the first 25 residues of ACE2 containing the leader sequence that direct ACE2 to the plasma membrane. This is followed by a 3xHA tag linked to the remainder of ACE2 (20-805) and a C-terminal sfGFP. Both 3xHA and sfGFP fusions are separated from ACE2 by flexible 3xGGGGS linkers. (B) The ACE2 fusion protein is designed to be embedded in the plasma membrane where it can perform extracellular carboxypeptidase-mediated metabolism and its levels can be detected by cell staining with antibodies to HA. (C) Lysates from untransfected or 3xHA-ACE2-sfGFP-transfected HEK293 cells were analyzed by automated Jess capillary immunoassay using antibodies to HA, GFP, and two ACE2 antibodies. (D) Confocal fluorescence microscopy of HEK cells transfected with 3xHA-ACE2-sfGFP and stained with HA and the nuclear stain DAPI. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/37644110), licensed under a CC-BY license. Not internally tested by R&D Systems.](http://images.novusbio.com/fullsize/af933_human-ace-2-ectodomain-affinity-purified-polyclonal-ab-30820241044556.jpg)
![N/A IL-6 [HRP]](http://images.novusbio.com/fullsize/elisa/DATA_IL6_R6000_ELISA_1084.jpg "N/A IL-6 [HRP]")
![N/A IL-6 [HRP]](http://images.novusbio.com/fullsize/elisa/IL-6_PR6000_ELISA_434.jpg)
![Immunocytochemistry/Immunofluorescence: CD11b Antibody - BSA Free [NB110-89474] - Raw264.7 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.05% Triton X-100 in PBS for 5 minutes. The cells were incubated with CD11b Antibody (NB110-89474) at 1ug/ml overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:1000 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.](http://images.novusbio.com/fullsize/CD11b-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB110-89474-img0031.jpg "Immunocytochemistry/Immunofluorescence: CD11b Antibody - BSA Free [NB110-89474] - Raw264.7 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.05% Triton X-100 in PBS for 5 minutes. The cells were incubated with CD11b Antibody (NB110-89474) at 1ug/ml overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:1000 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.")
![Immunocytochemistry/Immunofluorescence: CD11b Antibody - BSA Free [NB110-89474] - Raw264.7 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.05% Triton X-100 in PBS for 5 minutes. The cells were incubated with CD11b Antibody conjugated to Alexa Fluor 488 (NB110-89474AF488) at 5 ug/ml for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.](http://images.novusbio.com/fullsize/CD11b-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB110-89474-img0028.jpg)
![Western Blot: CD11b Antibody - BSA Free [NB110-89474] - Western Blot detection of CD11b in RAW 264.7 whole cell lysates using [NB110-89474].](http://images.novusbio.com/fullsize/CD11b-Antibody---BSA-Free-Western-Blot-NB110-89474-img0013.jpg)
![Immunocytochemistry/Immunofluorescence: CD11b Antibody - BSA Free [NB110-89474] - Staining of mouse pancreas using [NB110-89474] at 1:400 dilution. Nuclei counterstained with 4',6-diamidino-2-phenylindole (DAPI) (blue). ICC/IF image submitted by a verified customer review.](http://images.novusbio.com/fullsize/CD11b-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB110-89474-img0010.jpg)
![Flow (Cell Surface): CD11b Antibody - BSA Free [NB110-89474] - Surface staining of CD11b in CT26 colorectal carcinoma tumor model. Using Alexa Fluor 405 conjugated version of the antibody (NB110-89474AF405). Image from verified customer review.](http://images.novusbio.com/fullsize/CD11b-Antibody-BSA-Free-Flow-Cell-Surface-NB110-89474-img0033.jpg)
![Immunocytochemistry/Immunofluorescence: CD11b Antibody - BSA Free [NB110-89474] - Raw264.7 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.05% Triton X-100 in PBS for 5 minutes. The cells were incubated with CD11b Antibody conjugated to Alexa Fluor 647 (NB110-89474AF647) at 5 ug/ml for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.](http://images.novusbio.com/fullsize/CD11b-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB110-89474-img0029.jpg)
![Immunocytochemistry/Immunofluorescence: CD11b Antibody - BSA Free [NB110-89474] - Raw264.7 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.05% Triton X-100 in PBS for 5 minutes. The cells were incubated with CD11b Antibody conjugated to DyLight 650 (NB110-8947C) at 5 ug/ml for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.](http://images.novusbio.com/fullsize/CD11b-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB110-89474-img0030.jpg)
![Immunocytochemistry/Immunofluorescence: CD11b Antibody - BSA Free [NB110-89474] - CD11b Antibody [NB110-89474] - CD11b antibody [NB110-89474] was tested in Raw264.7 cells with DyLight 488 (green). Nuclei and alpha-tubulin were counterstained with 4',6-diamidino-2-phenylindole (DAPI) (blue) and DyLight 550 (red).](http://images.novusbio.com/fullsize/CD11b-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB110-89474-img0009.jpg)
![Immunohistochemistry: CD11b Antibody - BSA Free [NB110-89474] - Immunohistochemical analysis of CD11b in human renal cancer with [NB110-89474] using 3,3'-Diaminobenzidine (DAB) with hematoxylin counterstain.](http://images.novusbio.com/fullsize/CD11b-Antibody---BSA-Free-Immunohistochemistry-NB110-89474-img0011.jpg)
![Immunohistochemistry-Frozen: CD11b Antibody - BSA Free [NB110-89474] - Immunohistochemical analysis of frozen sections of mouse spleen using [NB110-89474]. IHC-Fr image submitted by a verified customer review.](http://images.novusbio.com/fullsize/CD11b-Antibody---BSA-Free-Immunohistochemistry-Frozen-NB110-89474-img0021.jpg)
![Flow (Cell Surface): CD11b Antibody - BSA Free [NB110-89474] - CD11b Antibody [NB110-89474] - A surface stain was performed on Raw264.7 cells with DyLight 550-conjugated [NB110-89474R] (blue) and a matched isotype control (orange). Cells were incubated in an antibody dilution of 10 ug/mL for 20 minutes at room temperature. Both antibodies were conjugated to DyLight 550.](http://images.novusbio.com/fullsize/CD11b-Antibody-BSA-Free-Flow-Cell-Surface-NB110-89474-img0022.jpg)
![Flow (Cell Surface): CD11b Antibody - BSA Free [NB110-89474] - An intracellular stain was performed on THP-1 cells with CD11b NB110-89474 (blue) and a matched isotype control NBP2-24891 (orange). 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 (SA5-10033, Thermo Fisher).](http://images.novusbio.com/fullsize/CD11b-Antibody-BSA-Free-Flow-Cell-Surface-NB110-89474-img0032.jpg)
![Simple Western: CD11b Antibody - BSA Free [NB110-89474] - Specific band for Cd11b in 1.0 mg/mL of Dentate Gyrus from Rat Brain. [NB110-89474] was used at a dilution of 1:50. This experiment was performed under reducing conditions using the 12-230 kDa separation system. Simple Western image submitted by a verified customer review.](http://images.novusbio.com/fullsize/CD11b-Antibody---BSA-Free-Simple-Western-NB110-89474-img0012.jpg)
![Dual RNAscope ISH-IHC: CD11b Antibody - BSA Free [NB110-89474] - Formalin-fixed paraffin-embedded tissue sections of human lymph node were probed for CD11b mRNA (ACD RNAScope Probe, catalog #555098; Fast Red chromogen, ACD catalog # 322750). Adjacent tissue section was processed for immunohistochemistry using Rabbit Polyclonal (Novus Biologicals catalog #NB110-89474) at 1:50 dilution with 1 hour incubation at room temperature followed by incubation with anti-rabbit IgG VisUCyte HRP Polymer Antibody (Catalog # VC003) and DAB chromogen (yellow-brown). Tissue was counterstained with hematoxylin (blue). Specific staining was localized to lymphocytes.](http://images.novusbio.com/fullsize/CD11b-Antibody---BSA-Free-Dual-RNAscope-ISH-IHC-NB110-89474-img0025.jpg)
![Dual RNAscope ISH-IHC: CD11b Antibody - BSA Free [NB110-89474] - CD14 mRNA (red) and CD11b protein (green) were detected in formalin-fixed paraffin-embedded tissue sections of human malignant lymph node. ACD's Integrated Co-Detection Workflow was performed using ACD RNAScope Probe Hs-CD14 and CD11b antibody at 1:200 dilution. Tissue was stained on Leica Bond RX using RNAscope (TM) 2.5 LS Reagent Kit-RED, BOND Polymer Refine Detection (DAB) and Hematoxylin, BOND Polymer Refine Red Detection and Hematoxylin and RNA scope (TM) 2.5 LS Green Accessory Pack. Tissue was counterstained with 50% hematoxylin (blue).](http://images.novusbio.com/fullsize/CD11b-Antibody---BSA-Free-Dual-RNAscope-ISH-IHC-NB110-89474-img0026.jpg)
![Western Blot: CD11b Antibody - BSA Free [NB110-89474] - Immunodensities of (a) CD11b, (b) GFAP & (c) NF-kappa B (p65) proteins with representative immunoblots in striatum from Munc18-OE (n = 5) & wild-type (n = 5) mice. Bar graphs are ratios of optical densities of our proteins of interest to beta -actin (42 kDa band), expressed as immunoreactivity in percentage of mean value of the WT group (100%). No differences were detected between groups for any of the analyzed proteins. Right panels are representative immunoblots for target proteins & beta -actin which included Munc18-OE (OE) & wild-type (WT) mice samples. The molecular masses were estimated from referenced standards. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25069615), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-89474_rabbit-polyclonal-cd11b-antibody-31020241535670.jpg)
![Immunohistochemistry: CD11b Antibody - BSA Free [NB110-89474] - Comparison of Ki-67 or CD11b immunoreactivity of Aldara-treated dorsal skin samples of C57BL/6 mice using OP or MP. Nuclear proliferation marker Ki-67 immunostaining on OP (a) & MP (b) dorsal skin tissue samples at 400x magnification. Dermal dendritic cells were labelled with anti-CD11b antibody on OP (c) & MP samples (d) at 400x magnification. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30842501), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-89474_rabbit-polyclonal-cd11b-antibody-310202415384158.jpg)
![Immunohistochemistry: CD11b Antibody - BSA Free [NB110-89474] - Comparison of Ki-67 or CD11b immunoreactivity of Aldara-treated dorsal skin samples of C57BL/6 mice using OP or MP. Nuclear proliferation marker Ki-67 immunostaining on OP (a) & MP (b) dorsal skin tissue samples at 400x magnification. Dermal dendritic cells were labelled with anti-CD11b antibody on OP (c) & MP samples (d) at 400x magnification. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30842501), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-89474_rabbit-polyclonal-cd11b-antibody-31020241539450.jpg)
![Western Blot: CD11b Antibody - BSA Free [NB110-89474] - Immunodensities of (a) CD11b, (b) GFAP & (c) NF-kappa B (p65) proteins with representative immunoblots in cerebral cortex from Munc18-OE (n = 5) & wild-type (n = 5) mice. Bar graphs are ratios of optical densities of our proteins of interest to beta -actin (42 kDa band), expressed as immunoreactivity in percentage of the mean value of the WT group (100%). CD11b was significantly decreased in Munc18-OE mice compared to the WT (t = 3.01; P <0.05). No differences between groups were observed in the levels of GFAP or NF-kappa B. Right panels are representative immunoblots for target proteins & beta -actin which included Munc18-OE (OE) & wild-type (WT) mice samples. The molecular masses were estimated from referenced standards. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25069615), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-89474_rabbit-polyclonal-cd11b-antibody-310202415394511.jpg)
![Immunocytochemistry/ Immunofluorescence: CD11b Antibody - BSA Free [NB110-89474] - CD11b staining in IMhu. Cells were stained with antibodies against the CD11b surface antigen. (A) Panel A shows positive staining for CD11b & (B) panel B shows nuclear DAPI staining. Magnitude 40×. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31096716), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-89474_rabbit-polyclonal-cd11b-antibody-310202415291998.jpg)
![Western Blot: FXC1 Overexpression Lysate (Adult Normal) [NBL1-10870] Left-Empty vector transfected control cell lysate (HEK293 cell lysate); Right -Over-expression Lysate for FXC1.](http://images.novusbio.com/fullsize/FXC1-Overexpression-Lysate-Adult-Normal-Western-Blot-NBL1-10870-img0002.jpg "Western Blot: FXC1 Overexpression Lysate (Adult Normal) [NBL1-10870] Left-Empty vector transfected control cell lysate (HEK293 cell lysate); Right -Over-expression Lysate for FXC1.")
![Simple Western: Mre11 Antibody [NB100-142] - Image shows a specific band for Mre11 in 0.5 mg/mL of HeLa lysate. A band appears at the theoretical molecular weight of 81 kDa for this product. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/Mre11-Antibody-Simple-Western-NB100-142-img0010.jpg "Simple Western: Mre11 Antibody [NB100-142] - Image shows a specific band for Mre11 in 0.5 mg/mL of HeLa lysate. A band appears at the theoretical molecular weight of 81 kDa for this product. This experiment was performed under reducing conditions using the 12-230 kDa separation system.")
![Immunocytochemistry/Immunofluorescence: Mre11 Antibody [NB100-142] - IF analysis of Mre11 on HeLa. Image from verified customer review.](http://images.novusbio.com/fullsize/Mre11-Antibody-Immunocytochemistry-Immunofluorescence-NB100-142-img0009.jpg)
![Immunohistochemistry: Mre11 Antibody [NB100-142] - Immunohistochemical staining of MRE11 in a human epidermis cross section.](http://images.novusbio.com/fullsize/Mre11-Antibody-Immunohistochemistry-NB100-142-img0004.jpg)
![Western Blot: Mre11 Antibody [NB100-142] - Western blot analysis of Mre11 on 50 ug of HeLa and MEF lysates, displaying bands at the molecular weight of 81 kDa.](http://images.novusbio.com/fullsize/Mre11-Antibody-Western-Blot-NB100-142-img0005.jpg)
![Immunocytochemistry/Immunofluorescence: Mre11 Antibody [NB100-142] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton X-100. The cells were incubated with anti-Mre11 [NB100-142] at a 1:500 dilution overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:500 dilution. Actin was detected with Phalloidin 568 (Red) at a 1:200 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/Mre11-Antibody-Immunocytochemistry-Immunofluorescence-NB100-142-img0011.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: Mre11 Antibody [NB100-142] - TIG-1 human primary fibroblasts, whole cell lysate (30 ug). Image from verified customer review.](http://images.novusbio.com/fullsize/Mre11-Antibody-Knockdown-Validated-NB100-142-img0008.jpg)
![Western Blot: Mre11 Antibody [NB100-142] - MRE11 associates with the DS region of OriP.A) DNA affinity purification assays were performed with Raji nuclear extracts & DNA templates derived from DS wt, DS nm-, or delta DS. Input & template bound proteins were analyzed by Western blot with antibodies to TRF2, MRE11, EBNA1, PCNA, & PARP1, as indicated. B) Schematic of template DNA used for DNA affinity purification in A, & their respective protein binding sites. C) ChIP assays to monitor EBNA1, TRF2, & MRE11 binding at OriP wt or OriP nm- in transfected 293 cells. Immunoprecipitated DNA was quantified by real time PCR relative to total input DNA recovered for each transfected cell. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/18040525), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-142_rabbit-polyclonal-mre11-antibody-310202415384114.jpg)
![Western Blot: Mre11 Antibody [NB100-142] - Immunoblotting analysis of IR-induced AKT (Ser473) activation. (A) The levels of AKT activation were measured by AKT Ser473 phosphorylation in 293T, 293T/eIF3f & 293T/eIF3f-hMSH4 cells treated with 10 Gy IR in comparison to untreated controls. Levels of p53 Ser15 phosphorylation & the total protein levels of AKT, hMRE11 & p53 were also analyzed. alpha -tubulin was used as a loading control. (B) The levels of Chk2 activation (Chk2 Thr68 phosphorylation) in 293T, 293T/eIF3f & 293T/eIF3f-hMSH4 cells in response to 10 Gy IR. Cell lysates were prepared at 1 hr post IR treatment. Untreated cells were analyzed as controls, while alpha -tubulin was used as a loading control. Image collected & cropped by CiteAb from the following publication (//molecular-cancer.biomedcentral.com/articles/10.1186/1476-4598-12-51), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-142_rabbit-polyclonal-mre11-antibody-310202415293334.jpg)
![Western Blot: Mre11 Antibody [NB100-142] - The DNA damage response at telomeres uncapped through TRF2 depletion does not require BRCA1 or CtIPImmortalized Brca1F/− MEFs were infected with retroviruses expressing the indicated shRNAs and/or Cre recombinase, followed by selection with puromycin for 72 h. Cell extracts were prepared 48 h later & analysed by Western blotting as indicated. SMC1 & tubulin were used as loading controls. *non-specific band.Cells treated as in (A) were fixed 48 h after selection & stained with an anti-53BP1 antibody (green). Telomeres were visualized with a Cy3-conjugated (CCCTAA)3-PNA probe (red). Yellow arrowheads point to 53BP1 foci that co-localize with telomeres.Quantification of TIFs in cells treated as in (B). A minimum of 200 nuclei were scored for each sample. Error bars represent SD of two independent experiments. P-values were calculated using an unpaired two-tailed t-test. *P ≤ 0.05; NS, P > 0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25582120), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-142_rabbit-polyclonal-mre11-antibody-31020241554548.jpg)
![Western Blot: Mre11 Antibody [NB100-142] - MRE11 & NBS1 contribute to OriP replication & EBV episome stability.A) D98/HR1 cells were transfected with siRNA for MRE11 or NBS1, or Luciferase control & assayed by immuno-blot (IB) with antibodies specific for MRE11 (left pane) or NBS1 (right panel), or PCNA (lower panel) as a loading control. B) Transient DNA replication assays of OriP-containing plasmids were analyzed by Southern blot. D98/HR1 cells were transfected with OriP plasmid & siRNA for either MRE11, NBS1, or luciferase control (as indicated above each lane). Hirt extracted plasmid DNA was digested with DpnI plus BamHI (top panel) or BamHI only (lower panel) & probed with OriP specific probes. DNA was quantified by PhosphorImager analysis & the replication value was determined as the ratio of DpnI/BamHI to BamHI recovered products. Quantification shown below is a summary of at least four independent replication assays (data not shown). C)) EBV episomes from latently infected D98/HR1 cells were analyzed by pulse field electrophoresis & Southern blotting after transfection of siRNA for control (siLuc), MRE11, or NBS1. Raji cells were used as a control for EBV episome size & abundance. The percentage of EBV episomes relative to the EBV DNA retained in the well is calculated below. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/18040525), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-142_rabbit-polyclonal-mre11-antibody-310202416574.jpg)
![Western Blot: Mre11 Antibody [NB100-142] - Evidence that MRE11 & NBS1 are required for EBV episome maintenance.A) OriP plasmid maintenance assays were performed in MRE11 mutant (ATLD3) & reconstituted (ATLD3/wtMRE11) cell lines (left panel) or NBS1 mutant (GM7166) & reconstituted (GM7166/wtNBS1) cell lines (right panel). Plasmids containing OriP & EBNA1 were monitored by Southern blotting of Hirt lysates at 1 (lower panel) & 7 (upper panel) days post-transfection. Phosphorimager quantification of four independent experiments as shown in panal A where maintenance is measured as the ratio of day 7 to day 1 for OriP plasmid detection is shown below. B) EBV transformed B-lymphocytes were analyzed by PFG & Southern blotting for the presence of episomal forms of the EBV genome. Raji, Namalwa, NBS1 (GM15808), NBS1 (GM07078), LCL3472, & LCLAW7 DNA was loaded at equal concentrations & analyzed by ethidium staining of PFG (lower panel) or by Southern blot (upper panel) with EBV specific probe. C) Western blot of the same cell lines used for PFG analysis shown in panel B was probed with antibodies specific for NBS1 (antibody 143 & antibody 277), MRE11, or loading control Actin. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/18040525), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-142_rabbit-polyclonal-mre11-antibody-31020241612675.jpg)
![Western Blot: Mre11 Antibody [NB100-142] - Involvement of CBP & p300 in the transcription of the BRCA1 & RAD51 genes.(A) Down-regulation of BRCA1 & RAD51 proteins upon depletion of CBP and/or p300. H1299 cells were transfected for 48 hr with non-targeting (siNT), CBP (siCBP), p300 (sip300), or CBP+p300 (siC+p) siRNAs. The cells were harvested & whole cell extracts were subjected to immunoblotting. (B, C) Reduction of BRCA1 & RAD51 transcripts in CBP- & p300-depleted cells. H1299 cells were transfected for 48 hr with non-targeting (siNT), CBP (siCBP), p300 (sip300), or CBP+p300 (siC+p) siRNAs. Cells were harvested & subjected to quantitative real-time PCR for the detection of BRCA1 (B) & RAD51 (C) mRNAs. Expression levels were normalized against the levels of GAPDH mRNA. Data represent the mean ± SD. (D) H1299 cells were transfected for 48 hr with non-targeting (siNT), CBP (siCBP), p300 (sip300), or CBP+p300 (siC+p) siRNAs, & stained with propidium iodide (PI). The percentage of cells in each cell cycle phase was determined by FACS. Percentages of cells in G1, S, & G2/M are shown. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23285190), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-142_rabbit-polyclonal-mre11-antibody-310202415525210.jpg)
![Immunocytochemistry/Immunofluorescence: mediator of cell motility 1 Antibody [NBP3-23408] - Immunocytochemical labeling of mediator of cell motility 1 in rabbit spleen fibroblasts that were fixed in paraformaldehyde and permeabilized with NP-40. The cells were probed with the mediator of cell motility 1 (N-terminal Region) NBP3-23408, then the antibody was detected using goat anti-rabbit DyLight(R) 594. The antibody was used in the absence (left) or presence (right) of it's blocking peptide.](http://images.novusbio.com/fullsize/nbp3-23408_rabbit-mediator-of-cell-motility-1-pab-119202316331614.jpg "Immunocytochemistry/Immunofluorescence: mediator of cell motility 1 Antibody [NBP3-23408] - Immunocytochemical labeling of mediator of cell motility 1 in rabbit spleen fibroblasts that were fixed in paraformaldehyde and permeabilized with NP-40. The cells were probed with the mediator of cell motility 1 (N-terminal Region) NBP3-23408, then the antibody was detected using goat anti-rabbit DyLight(R) 594. The antibody was used in the absence (left) or presence (right) of it's blocking peptide.")
![Western Blot: mediator of cell motility 1 Antibody [NBP3-23408] - Western blot analysis of mediator of cell motility 1 expression in adult mouse heart (lane 1 & 4), mouse C2C12 cells (lane 2 & 5), and rabbit spleen fibroblast cells (lane 3 & 6). The blot was probed with anti-mediator of cell motility 1 (N-terminal region) (NBP3-23408; lanes 1-6) in the presence (lanes 4-6) or absence (lanes 1-3) of mediator of cell motility 1 blocking peptide.](http://images.novusbio.com/fullsize/nbp3-23408_rabbit-mediator-of-cell-motility-1-pab-199202312403717.jpg)
![Immunohistochemistry: mediator of cell motility 1 Antibody [NBP3-38565] - Immunohistochemistry analysis of paraffin-embedded Rat brain using mediator of cell motility 1 Rabbit pAb at dilution of 1:100 (40x lens). Microwave antigen retrieval performed with 0.01M PBS Buffer (pH 7.2) prior to IHC staining.](http://images.novusbio.com/fullsize/nbp3-38565_rabbit-mediator-of-cell-motility-1-pab-101220241243940.jpg "Immunohistochemistry: mediator of cell motility 1 Antibody [NBP3-38565] - Immunohistochemistry analysis of paraffin-embedded Rat brain using mediator of cell motility 1 Rabbit pAb at dilution of 1:100 (40x lens). Microwave antigen retrieval performed with 0.01M PBS Buffer (pH 7.2) prior to IHC staining.")
![Immunohistochemistry: mediator of cell motility 1 Antibody [NBP3-38565] - Immunohistochemistry analysis of paraffin-embedded Human prostate using mediator of cell motility 1 Rabbit pAb at dilution of 1:100 (40x lens). Microwave antigen retrieval performed with 0.01M PBS Buffer (pH 7.2) prior to IHC staining.](http://images.novusbio.com/fullsize/nbp3-38565_rabbit-mediator-of-cell-motility-1-pab-101220241252817.jpg)
![Western Blot: mediator of cell motility 1 Antibody [NBP3-38565] - Western blot analysis of various lysates using mediator of cell motility 1 Rabbit pAb at 1:1000 dilution.Secondary antibody: HRP-conjugated Goat anti-Rabbit IgG (H+L) at 1:10000 dilution.Lysates/proteins: 25ug per lane.Blocking buffer: 3% nonfat dry milk in TBST.Detection: ECL Enhanced Kit.Exposure time: 60s.](http://images.novusbio.com/fullsize/nbp3-38565_rabbit-mediator-of-cell-motility-1-pab-1012202411572650.jpg)
![Immunohistochemistry-Paraffin: mediator of cell motility 1 Antibody [NBP1-88269] - Staining of human skeletal muscle shows strong cytoplasmic positivity in myocytes.](http://images.novusbio.com/fullsize/mediator-of-cell-motility-1-Antibody-Immunohistochemistry-Paraffin-NBP1-88269-img0005.jpg "Immunohistochemistry-Paraffin: mediator of cell motility 1 Antibody [NBP1-88269] - Staining of human skeletal muscle shows strong cytoplasmic positivity in myocytes.")
HAF017). Specific bands were detected for TrkB at approximately 90-100 and 140 kDa (as indicated). This experiment was conducted under reducing conditions and using 
NL001) and counterstained with DAPI (blue). Specific staining was localized to neuronal processes and cell bodies. View our protocol for 
HAF109). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system." class="big_thumb" />
![Flow Cytometry: GL7 (T and B Cell Activation Marker) Antibody (GL-7) [NBP2-00362] - Analysis using the Biotin conjugate of NBP2-00362. Staining of 3-day unstimulated (left) and 3-day ConA activated (right) BALB/c splenocytes with 0.5 ug of Rat IgM Isotype Control Biotin (open histogram) or 0.25ug of Anti-Human/Mouse GL7 (T and B Cell Activation Marker) Biotin (filled histogram) followed by Streptavidin PE. Total viable cells were used for analysis.](http://images.novusbio.com/fullsize/GL7-T-and-B-Cell-Activation-Marker-Antibody-GL-7-Flow-Cytometry-NBP2-00362-img0003.jpg "Flow Cytometry: GL7 (T and B Cell Activation Marker) Antibody (GL-7) [NBP2-00362] - Analysis using the Biotin conjugate of NBP2-00362. Staining of 3-day unstimulated (left) and 3-day ConA activated (right) BALB/c splenocytes with 0.5 ug of Rat IgM Isotype Control Biotin (open histogram) or 0.25ug of Anti-Human/Mouse GL7 (T and B Cell Activation Marker) Biotin (filled histogram) followed by Streptavidin PE. Total viable cells were used for analysis.")
![Flow Cytometry: GL7 (T and B Cell Activation Marker) Antibody (GL-7) [NBP2-00362] - Staining of 3-day unstimulated (left) and 3-day ConA-stimulated (right) BALB/c splenocytes with 0.25 ug of Rat IgM kappa Isotype Control Purified (open histogram) or 0.25 ug of Anti-Human/Mouse GL7 (T and B Cell Activation Marker) Purified (filled histogram) followed by Anti-Rat IgM PE.](http://images.novusbio.com/fullsize/GL7-T-and-B-Cell-Activation-Marker-Antibody-GL-7-Flow-Cytometry-NBP2-00362-img0001.jpg)
