| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB110-67828 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB300-221SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB600-308-1mg | |||
| BSA Free | NB600-308SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-56736SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-2324SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP2-55551-25ul | |||
![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)
![Analysis of cell line lysates probed with mouse mAb to GAPDH (theoretical molecular weight: 36 kDa), NB300-221, dilution 1:2,000: [1] protein standard, [2] HEK293, [3] HeLa, [4] SH-SY5Y, [5] COS1, [6] NIH-3T3, and [7] C6 cells. The GAPDH antibody reveals a single band at ~37 kDa in all cell lines. GAPDH is a house keeping protein, the level of which is relatively unaffected by most experimental manipulations, and, as a result, this antibody has been widely used as a western blotting loading control.](http://images.novusbio.com/fullsize/GAPDH-Antibody-1D4-Western-Blot-NB300-221-img0008.jpg)
![Western Blot: GAPDH Antibody (1D4) [NB300-221] - Notch1, ApoER2 & Dab1 colocalize in hippocampal neurons. (A) Representative image of fluorescent immunolabeling shows that Notch1 is localized in a subset of CA3 neurons, co-expressing Dab1 & ApoER2 (magnified insert). ApoER2 is highly expressed in all CA3 neurons. (B) Fluorescent immunolabeling shows the distribution of Notch1 & Dab1 as compared to Arc/Arg3.1 in CA3 neurons. (B′) Close up of a dendrite showing colocalization of the three proteins (white arrowheads). (C) Western blot analysis on immunoprecipitated samples from whole hippocampal lysate shows that Notch1 displays a strong interaction with Dab1 whereas Notch1 & ApoER2 interaction appears weaker in the preparation (n = 4 independent experiments). (D) Immunolabeling on immunoprecipitated samples from whole cortical lysates show that Notch1 & Dab1 interact. ApoER2 is bound to both Notch1 & Dab1 (n = 3 independent experiments). (E) Co-IP from synaptosomal membrane fractions reveals a stronger interaction between Notch1 & ApoER2, which is reduced in the N1cKO (n = 3 independent pulldowns). In (C–E) GAPDH is used as a loading control for the inputs & to detect contamination in the IP samples. Scale bar in (A) is 50 μm & (B) 25 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26635527), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-221_mouse-monoclonal-gapdh-antibody-1d4-imgenex-img-5019a-310202416205131.jpg)
![Western Blot: GAPDH Antibody (1D4) [NB300-221] - Reduced expression of UNC5A in FancC−/− cells. a Reduced expression of Unc5A in brain cortex of FancC−/− mice compared to wild-type littermates. Western blotting was performed with the indicated antibodies. Each lane represents a different animal (WT: n = 6; FancC−/−: n = 8). b Bar graph represents ratio of Unc5A normalized to tubulin from WT (n = 6) & FancC−/− mice (n = 8). c Bar graph representation of UNC5A expression normalized to Sdha & Tbp from wild-type (WT) & FancC−/−-derived fibroblasts (n = 3). RLU: Relative light units. d–f HEK293T cells were transfected with UNC5AICD, FANCE & FANCC constructs expressing full-length FANCC (in d), FANCC1–306 (in e) or FANCC307–558 (in f). Constructs were transfected at a molecular ratio of 1:1:1 or with 10 times the molar amount of FANCE, FANCC or UNC5AICD as indicated in the figure. The total amount of transfected plasmid was equalized for all strategies with control empty vectors. Representative immunoblots performed with anti-HA (UNC5AICD), anti-FANCC, anti-FANCE or anti-GAPDH antibodies are shown. Arrows indicate appropriate protein bands. Bar graphs represent the mean fold change ± SEM of UNC5A protein levels normalized to GAPDH compared to 1:1:1 transfection controls in at least 4 separate experiments. *p < 0.05; **p < 0.005 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30213274), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-221_mouse-monoclonal-gapdh-antibody-1d4-imgenex-img-5019a-310202416203715.jpg)
![Western Blot: GAPDH Antibody (1D4) [NB300-221] - Depletion of RAD21 & other cohesin subunits leads to differentiation of ESCs.(A): qPCR analysis of esiRNA knock-down efficiency for indicated genes (48 h RNAi, n = 3, error bars denote s.d. & *, ** indicate p<0.05 & 0.01 respectively). Transfection of a non-targeting esiRNA (Luc) was used as a control. Numbers adjacent to the gene names indicate independent, non-overlapping esiRNAs transfected. (B): Western Blot analysis of esiRNA knock-down efficiency for indicated genes (48 h RNAi; esi-1 & esi-2 indicate independent, non-overlapping esiRNAs transfected). Transfection of a non-targeting esiRNA (Luc) was used as a control. GAPDH served as a protein loading control. (C): Alkaline phosphatase staining of ESCs, which had been transfected with esiRNAs targeting RAD21, SMC1a & SMC3 (72 h post RNAi) showed a strong differentiation phenotype compared to a control (Luc). Nanog depletion served as a positive control for ESC differentiation. Scale bars correspond to 100 µm. (D): Quantification of alkaline phosphatase staining (n = 3) separated into undifferentiated (green), mixed (yellow) & differentiated colonies (red). (E+F): qPCR validation of expression changes of (E) stem cell maintenance genes & (F) lineage marker genes upon knock-down of RAD21 (two independent esiRNAs) & Luc control (48 h RNAi, n = 3, error bars denote s.d. & *, **, *** indicate p<0.05, 0.01 & 0.001 respectively). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/21589869), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-221_mouse-monoclonal-gapdh-antibody-1d4-imgenex-img-5019a-310202416205163.jpg)
![Western Blot: GAPDH Antibody (1D4) [NB300-221] - Application of the approach to other cell lines. (A) HT1080 cells (2 × 105) & HeLa cells (1 × 105) were plated in the wells of a 12 well plate & the digitonin concentration required for optimal extraction of the cytosol was determined as in Figure1. (B) The remainder of the protocol from Figure 2 was then applied using 100 μg/ml digitonin as the optimal cytosolic extract in each case. An aliquot of each extract was then analyzed by 4-12% SDS PAGE followed by Western blotting & probing with antibodies to GAPDH, BiP & Histone H3 (Used as an alternative nuclear marker due to weakness of the Lamin A signal in HeLa cells). (C) Samples were analyzed by 4-12% SDS PAGE followed by staining with Coomassie blue & then silver staining showing the difference in protein composition of each sample. The bracket alongside the gels marks the position of Histones in the RIPA nuclear extract & the asterisk next to the silver stained gels denotes protein bands unique to the E-RIPA extracts. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/20003239), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-221_mouse-monoclonal-gapdh-antibody-1d4-imgenex-img-5019a-3102024162187.jpg)
![Western Blot: GAPDH Antibody (1D4) [NB300-221] - Role of the TRIM11-USP14 axis in cell growth & apoptosis. a Levels of endogenous TRIM11 in HCT116 cells grown at 43 °C for 0 or 90 min, or at 43 °C for 90 min, & then at 37 °C for 60 or 120 min. b, c Levels of endogenous TRIM11 (b), or Flag-TRIM11, the indicated proteasome subunits, & USP14 (c) in the SN & P fractions of HCT116 cells with & without heat shock at 43 °C for 90 min. d, g TRIM11 overexpression (d) or knockdown (g) HCT116 cells & the corresponding control cells grown under unstressed, heat shock, & heat shock plus recovery conditions were analyzed for K48 polyUb conjugates & caspase-3 activation. e, f, h Apoptosis in TRIM11 overexpression (e, f) or knockdown (h) HCT116 cells, & the corresponding control HCT116 cells, treated with & without heat shock. i, j Caspase-3 activation (i) & apoptosis (j) in HCT116 cells expressing the indicated proteins and grown under normal or heat stress conditions. k–m K48 polyUb conjugates, caspase-3 activation (k), amyloid-like fibrils (l), & apoptosis (m) in HCT116 cells expressing the indicated proteins and grown under normal & heat stress conditions. In e, f, h, j, l, & m, data represent mean ± SEM (n = 3 unless otherwise indicated). *P < 0.05; **P < 0.01; ***P < 0.001. Uncropped blots are presented in Supplementary Fig. 14 Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-018-03499-z), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-221_mouse-monoclonal-gapdh-antibody-1d4-imgenex-img-5019a-310202416212324.jpg)
![Total cell lysates (20ug) with protein of interest tagged with GFP was loaded. Blotted with GFP antibody [HRP] NB600-308H, without any secondary antibody. Image from verified customer review.](http://images.novusbio.com/fullsize/GFP-Antibody-Western-Blot-NB600-308-img0036.jpg)
![Western Blot of GFP antibody. Lane 1: Wild type GFP (0.1 ug) was used to spike HeLa whole cell lysate. Lane 2: none. Load: 30 ug per lane.Primary antibody: GFP antibody at 1:1000 for overnight at 4C.Secondary antibody: IRDye800(TM) Goat-a-Rabbit IgG [H&L] MX10 at 1:10,000 for 45 min at RT.Block: 5% BLOTTO in PBS overnight at 4C.Predicted/Observed size: 27 kDa for epitope tag GFP. Other band(s): none.](http://images.novusbio.com/fullsize/GFP-Antibody-Western-Blot-NB600-308-img0032.jpg)
![Immunocytochemistry/ Immunofluorescence: GFP Antibody [NB600-308] - Myc is post-transcriptionally regulated by the IIS-GSK3 cascade.(A) Germaria from ovaries of ctrl, chicoRNAi, & bskRNAi driven by nos-Gal4 expressing LacZ under the control of myc endogenous promoter stained with anti-beta -galactosidase & anti-1B1. Scale bars, 10 μm. (B) A representative live imaging of germaria from flies expressing GFP-tagged Sgg under its endogenous promoter. Scale bar, 10 μm. (C) A germarium from wt flies endogenously expressing Myc-GFP stained with anti-GFP (green) & anti-p-GSK3 (red). Germarium regions are indicated. Myc protein highly corresponds to inhibited form of GSK3. Scale bar, 10 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31612862), licensed under a CC0-1.0 license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-308_rabbit-polyclonal-gfp-antibody-31020241529193.jpg)
![Immunocytochemistry/ Immunofluorescence: GFP Antibody [NB600-308] - Myc protein pattern in the ovary.(A) A representative low-magnification image of ovarioles from flies endogenously expressing Myc-GFP stained with anti-GFP, anti-1B1, & DAPI. Note that Myc level is low in early germarium stages, becomes high from germarium region 2B, & reduces from the stage-10 egg chamber. Scale bar, 50 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31612862), licensed under a CC0-1.0 license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-308_rabbit-polyclonal-gfp-antibody-310202415291968.jpg)
![Western Blot: GFP Antibody [NB600-308] - MISP interacts & co-localizes with IQGAP1. (a) HEK293T cells transiently overexpressing GFP-IQGAP1 & FLAG-MISP were used for co-immunoprecipitation experiments from both sides (GFP trap or FLAG M2 beads). (b) Endogenous immunoprecipitation using IQGAP1 antibody or control immunoglobulin (IgG) was carried out in HeLa cell lysates & MISP was detected in the eluate. (c) In vitro interaction between purified MBP-MISP & GST-IQGAP1 was detected by GST & MBP pull-down experiments. (d) Immunoprecipiation experiments showing that GFP-MISP binds endogenous IQGAP1 (upper panel) & MISP binds to IQGAP1 endogenously using specific antibodies (lower panel) in mitotically arrested (taxol & nocodazole, respectively) HeLa cell lysates. (a–d) Images were gained from the same Western blot membrane after cutting/cropping & presented with different exposure times or contrast enhancement for better presentation purposes. The dividing lane marks the grouping of images of the same (or different) membrane. Uncropped blots, where applicable, are included in Supplementary Fig. 4. (e) HeLa cells were immunostained for MISP & IQGAP1 & co-localization was visualized in mitosis in single-plane confocal images, scale bar: 5 μm. Lower pictures: After manual thresholding white spots mark the co-localizing areas in the merge images. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29679050), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-308_rabbit-polyclonal-gfp-antibody-310202416173520.jpg)
![Immunocytochemistry/ Immunofluorescence: GFP Antibody [NB600-308] - BRC-1 & BRD-1 are inter-dependent for localization.A) Co-localization between BRD-1::GFP (green) & TagRFP-T::BRC-1 (red) at late pachytene in live worms. Scale bar = 10 μm. B) Stills of germline nuclei from live worms expressing GFP::BRC-1 & mCherry::Histone H2B (mCherry::his-58; gfp::brc-1); merge & GFP channel; top two panels, respectively. GFP::BRC-1 expression in brd-1(ok1623) mutant at indicated meiotic stages. Bottom two panels show BRD-1::GFP localization in wild type & the brc-1(xoe4) mutant. Images are projections through half of the gonad. TZ = transition zone; EP = early pachytene; MP = mid pachytene; LP = late pachytene; DP = diplotene; DK = diakinesis. Scale bar = 5 μm. C) Immunoblot of whole worm extracts from indicated worms probed with anti-GFP & alpha -tubulin antibodies. Lane 1 = N2: wild type; Lane 2 = JEL515: gfp::brc-1; Lane 3 = JEL520: gfp::brc-1 brd-1(ok1623); Lane 4 = JEL744: brc-1(xoe4) brd-1::gfp; Lane 5 = JEL657: brd-1::gfp; Lane 6 = JEL678: brc-1(tm1145) brd-1::gfp. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30383767), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-308_rabbit-polyclonal-gfp-antibody-310202416165637.jpg)
![Western Blot: GFP Antibody [NB600-308] - BRC-1 & BRD-1 are inter-dependent for localization.A) Co-localization between BRD-1::GFP (green) & TagRFP-T::BRC-1 (red) at late pachytene in live worms. Scale bar = 10 μm. B) Stills of germline nuclei from live worms expressing GFP::BRC-1 & mCherry::Histone H2B (mCherry::his-58; gfp::brc-1); merge & GFP channel; top two panels, respectively. GFP::BRC-1 expression in brd-1(ok1623) mutant at indicated meiotic stages. Bottom two panels show BRD-1::GFP localization in wild type & the brc-1(xoe4) mutant. Images are projections through half of the gonad. TZ = transition zone; EP = early pachytene; MP = mid pachytene; LP = late pachytene; DP = diplotene; DK = diakinesis. Scale bar = 5 μm. C) Immunoblot of whole worm extracts from indicated worms probed with anti-GFP & alpha -tubulin antibodies. Lane 1 = N2: wild type; Lane 2 = JEL515: gfp::brc-1; Lane 3 = JEL520: gfp::brc-1 brd-1(ok1623); Lane 4 = JEL744: brc-1(xoe4) brd-1::gfp; Lane 5 = JEL657: brd-1::gfp; Lane 6 = JEL678: brc-1(tm1145) brd-1::gfp. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30383767), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-308_rabbit-polyclonal-gfp-antibody-31020241616050.jpg)
![Immunocytochemistry/ Immunofluorescence: GFP Antibody [NB600-308] - Other IIS components are not altered by bsk RNAi.(A) Confocal images for germaria expressing Chico-GFP, myc-Dp110 or PDK1-GFP in the background of ctrl or bskRNAi from ovaries stained with anti-GFP or anti-myc. Scale bars, 10 μm. (B) Ovaries expressing LacZ driven by the puc promoter stained with anti-beta -galactosidase, anti-1B1, & DAPI. Note that JNK activity is moderately induced in late germarium & decreased in the following stages, while JNK activity is much stronger in follicle cells of a maturing egg. Scale bars, 20 μm. (C) Germaria from ovaries of ctrl & bskRNAi driven by nos-Gal4 stained with anti-AKT & anti-1B1. Scale bars, 10 μm. (D) Quantification of AKT intensity from cysts in germarium region 2A & 2B of ovaries with ctrl & bskRNAi driven by nos-Gal4. Intensities are normalized to the value of ctrl at region 2B. n = 7 & 8 germaria for ctrl & bskRNAi, respectively. Error bars represent SEM. *p<0.005. (E) Visualization of the InR mRNA by FISH in germaria from ovaries of ctrl & bskRNAi driven by nos-Gal4. Note that InR mRNA level is decreased by bsk RNAi. Germaria are outlined with dotted lines. Scale bars, 10 μm. (F) Quantification of InR mRNA density in region 2A & 2B germ cells from ovaries with indicated genotypes. n = 9 germaria for each genotype. Error bars represent SEM. *p<0.005. (G) Quantification of relative Myc-GFP intensity in region 2B cysts of ovaries illustrated in Figure 5H. n = 10 germaria for each genotype. Error bars represent SEM. *p<0.005.10.7554/eLife.49309.017Figure 5—figure supplement 1—source data 1.Relative AKT intensity, InR mRNA density, & Myc-GFP intensity in the germarium.Relative AKT intensity, InR mRNA density, & Myc-GFP intensity in the germarium. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31612862), licensed under a CC0-1.0 license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-308_rabbit-polyclonal-gfp-antibody-31020241616189.jpg)
![Western Blot: GFP Antibody [NB600-308] - GFP Expression within A. thaliana upon infiltration with SWNT-PM-CytKH9/pDNA complexes.a Reporter construct design of transient GFP expression for the nucleus & mitochondria. b Representative confocal laser scanning microscopy images of A. thaliana root cells from a minimum of five seedlings for each condition (n = 5) 18 h post infiltration with SWNT-PM-CytKH9/pDNA complexes containing pDONR-35S-GFP or pDONR-Cox2-GFP reporter constructs for nuclear or mitochondrial expression, respectively. Mitochondria were stained with MitoTracker Red (CMXRos), & colocalization analysis was performed on GFP expression & MitoTracker signals. Scale bars represent 20 μm. c, d Representative western blots & their quantification from cytosolic (c) & mitochondrial (d) fractions isolated from approximately 60 seedlings 18 h post infiltration with SWNT NCs probed for GFP expression. Actin & cytochrome c were used as loading controls for cytosolic & mitochondrial proteins, respectively. Data points from five biological replicates (n = 5) are represented as the mean ± standard deviation. Statistical significance was determined by Brown-Forsythe & Welch one-way ANOVA test. For the cytosolic samples, P-values are 0.0027, & 0.0020 between DNA only & SWNT-PM-CytKH9, SWNT-PM-Cytcox, respectively, & 0.0253 between SWNT-PM-CytKH9 & SWNT-PM-Cytcox. For the mitochondrial samples, P-values are 0.0019, & 0.0333 between DNA only & SWNT-PM-CytKH9, & SWNT-PM-Cytcox, respectively, & 0.0359 between SWNT-PM-CytKH9 & SWNT-PM-Cytcox. ns – not statistically significant, *P < 0.05, **P < 0.01. Source data are provided as a Source Data file. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35577779), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-308_rabbit-polyclonal-gfp-antibody-310202416165624.jpg)
![Western Blot: GFP Antibody [NB600-308] - VGLL1 regulates MMP9 transcription in gastric cancer cells. (a,b) Viability (a) & invasion (b) assay of NUGC3 cells. Cells were treated with 20 nM siScramble (SC) or siMMP9 for 48 h, & then stained with sulforhodamine B. Data are presented as mean ±SD. n = 3; * p < 0.05 (Student’s t-test). (c) MMP9 mRNA expression regulation by VGLL1 in gastric cancer cells treated with siVGLL1 or siSC (control) was measured by qPCR. (d) Changes in MMP9 expression upon knockdown or overexpression of VGLL1 assayed by western blotting in NUGC3 cells. (e) IHC of VGLL1 & MMP9 expression in the liver & lungs of an in vivo metastasis mouse model using surgical resection of tumors. Scale bar, 200 µm. (f) Construction of various luciferase reporter systems under control of the MMP9 promoter. (g) MMP9 promoter activities of the reporter systems containing modified TEA-binding sites were measured in NUGC3 cells. n = 3; * p < 0.05 (Student’s t-test). (h) Effect of TEAD4 on VGLL1-regulated MMP9 transcriptional activity. NUGC3 cells treated with siSC or siTEAD4 for 24 h were transfected with MMP9-luc, Renilla-luc, pCDNA3.1, & pcDNA3.1-myc-VGLL1 vectors for 48 h. n = 3; * p < 0.05 (Student’s t-test). (i) Interaction between VGLL1 & TEAD4. Lysates of NUGC3 cells that were transfected with pcDNA3.1-myc-VGLL1 & pEGFP-N1-TEAD4 were immunoprecipitated using anti-IgG, anti-GFP, & anti-Myc antibodies. Protein expression was analyzed by immunoblotting. (j) ChIP assays while using nuclear extracts of NUGC3 cells treated with siTEAD4. The ChIP-enriched DNA was subjected to PCR. (k) Target genes of VGLL1 & YAP. NUGC3 cells were transfected with pcDNA3, pcDNA3-myc-VGLL1, or pcDNA3-myc-YAP, & the mRNA expression levels were analyzed by RT-PCR. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31816819), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-308_rabbit-polyclonal-gfp-antibody-31020241616054.jpg)
![Immunocytochemistry/Immunofluorescence: Rabbit GFP pAb [NB600-308] - Analysis of GFP in human Hs746T gastric cancer cell line. Image from a verified customer review.](http://images.novusbio.com/fullsize/antibody/nb600-308_rabbit-polyclonal-gfp-antibody-immunocytochemistry-immunofluorescence-2032025112942..png)
![Western Blot: RGS2 Antibody (4C4) [H00005997-M01] - Knockdown efficiencies of target proteins in HEK293 cells measured by Reverse Phase Protein Array (RPPA) and Western blotting (WB). Level of expression by WB and RPPA of targeted proteins in HEK293 cells transfected with siRNA targeting proteins of interest or non-silencing siRNA control (siCTR). Specific bands for WB and spots corresponding to the dilution of the dynamic range in RPPA are presented. Image collected and cropped by CiteAb from the following publication (//rbej.biomedcentral.com/articles/10.1186/1477-7827-11-100) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/RGS2-Antibody-4C4-Knockdown-Validated-H00005997-M01-img0011.jpg "<b>Genetic Strategies Validation. </b>Western Blot: RGS2 Antibody (4C4) [H00005997-M01] - Knockdown efficiencies of target proteins in HEK293 cells measured by Reverse Phase Protein Array (RPPA) and Western blotting (WB). Level of expression by WB and RPPA of targeted proteins in HEK293 cells transfected with siRNA targeting proteins of interest or non-silencing siRNA control (siCTR). Specific bands for WB and spots corresponding to the dilution of the dynamic range in RPPA are presented. Image collected and cropped by CiteAb from the following publication (//rbej.biomedcentral.com/articles/10.1186/1477-7827-11-100) licensed under a CC-BY license.")
![<b>Genetic Strategies Validation. </b>Western Blot: RGS2 Antibody (4C4) [H00005997-M01] - Specificity of antibodies. HEK293 cells lysates were analysed by Western blotting to test the specificity of antibodies. Image collected and cropped by CiteAb from the following publication (//rbej.biomedcentral.com/articles/10.1186/1477-7827-11-100) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/RGS2-Antibody-4C4-Western-Blot-H00005997-M01-img0012.jpg)
![Immunohistochemistry-Paraffin: RGS2 Antibody (4C4) [H00005997-M01] - Analysis of monoclonal antibody to RGS2 on formalin-fixed paraffin-embedded human tonsil. Antibody concentration 3 ug/ml.](http://images.novusbio.com/fullsize/RGS2-Antibody-4C4-Immunohistochemistry-Paraffin-H00005997-M01-img0005.jpg)
![Western Blot: RGS2 Antibody (4C4) [H00005997-M01] - RGS2 monoclonal antibody (M01), clone 4C4 Analysis of RGS2 expression in MCF-7.](http://images.novusbio.com/fullsize/RGS2-Antibody-4C4-Western-Blot-H00005997-M01-img0007.jpg)
![ELISA: RGS2 Antibody (4C4) [H00005997-M01] - Detection limit for recombinant GST tagged RGS2 is approximately 0.1ng/ml as a capture antibody.](http://images.novusbio.com/fullsize/RGS2-Antibody-4C4-ELISA-H00005997-M01-img0008.jpg)
![Western Blot: RGS2 Antibody (4C4) [H00005997-M01] - Specificity of antibodies. HEK293 cells lysates were analysed by Western blotting to test the specificity of antibodies. Image collected & cropped by CiteAb from the following publication (//rbej.biomedcentral.com/articles/10.1186/1477-7827-11-100), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/h00005997-m01_mouse-monoclonal-rgs2-antibody-4c4-310202415394536.jpg)
![Western Blot: RGS2 Antibody (4C4) [H00005997-M01] - Knockdown efficiencies of target proteins in HEK293 cells measured by Reverse Phase Protein Array (RPPA) & Western blotting (WB). A. Detection by RPPA of VCL & ERK2 in serial dilution of HEK293 cells transfected with siRNA targeting VCL (siVCL) or non-silencing siRNA control (siCTR). B. Linear regression was performed for ERK2 & VCL protein & Pearson correlation between dilution & the signal intensity was calculated for each condition of Figure 3A, with all p-values lower than 0.001. Signal intensities are expressed as mean of the replicates. C. Level of expression by WB & RPPA of targeted proteins in HEK293 cells transfected with siRNA targeting proteins of interest or non-silencing siRNA control (siCTR). Specific bands for WB & spots corresponding to the dilution of the dynamic range in RPPA are presented. Image collected & cropped by CiteAb from the following publication (//rbej.biomedcentral.com/articles/10.1186/1477-7827-11-100), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/h00005997-m01_mouse-monoclonal-rgs2-antibody-4c4-310202415482256.jpg)
![Immunocytochemistry/Immunofluorescence: RGS2 Antibody [NBP1-32284] - Methanol-fixed A549, using RGS2 antibody at 1:200 dilution.](http://images.novusbio.com/fullsize/RGS2-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-32284-img0002.jpg "Immunocytochemistry/Immunofluorescence: RGS2 Antibody [NBP1-32284] - Methanol-fixed A549, using RGS2 antibody at 1:200 dilution.")
![Immunohistochemistry-Paraffin: RGS2 Antibody [NBP1-32284] - Rat ovary. RGS2 antibody diluted at 1:500. Antigen Retrieval: Citrate buffer, pH 6.0, 15 min.](http://images.novusbio.com/fullsize/RGS2-Antibody-Immunohistochemistry-Paraffin-NBP1-32284-img0005.jpg)
![Western Blot: RGS2 Antibody [NBP1-32284] -Whole cell extract (30 ug) was separated by 12% SDS-PAGE, and the membrane was blotted with RGS2 antibody diluted at 1:1000. The HRP-conjugated anti-rabbit IgG antibody (NBP2-19301) was used to detect the primary antibody.](http://images.novusbio.com/fullsize/antibody/nbp1-32284_rabbit-polyclonal-rgs2-antibody-western-blot-289202385254..jpg)
![Western Blot: RGS2 Antibody [NBP1-32284] - Whole cell extract (30 ug) was separated by 12% SDS-PAGE, and the membrane was blotted with RGS2 antibody diluted at 1:1000. The HRP-conjugated anti-rabbit IgG antibody (NBP2-19301) was used to detect the primary antibody.](http://images.novusbio.com/fullsize/antibody/nbp1-32284_rabbit-polyclonal-rgs2-antibody-western-blot-289202385434..jpg)
![Western Blot: RGS2 Antibody [NB100-56736] - Western bot analysis of RGS2 in human heart lysate using RGS2 antibody at 2 ug/ml.](http://images.novusbio.com/fullsize/RGS2-Antibody-Western-Blot-NB100-56736-img0002.jpg "Western Blot: RGS2 Antibody [NB100-56736] - Western bot analysis of RGS2 in human heart lysate using RGS2 antibody at 2 ug/ml.")
![Immunohistochemistry: IRE1 alpha Antibody [NB100-2324] - XBP1 and TG2 deficiency promote increased IRE1a protein levels in cultured VSMCs and in neointima in situ. (D) Xbp1WT and Xbp1 delta WT and (E) Tgm2 WT and Tgm2 delta carotid artery sections were analyzed by IHC for total IRE1a. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0212235) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/IRE1-alpha-Antibody-Immunohistochemistry-NB100-2324-img0010.jpg "Immunohistochemistry: IRE1 alpha Antibody [NB100-2324] - XBP1 and TG2 deficiency promote increased IRE1a protein levels in cultured VSMCs and in neointima in situ. (D) Xbp1WT and Xbp1 delta WT and (E) Tgm2 WT and Tgm2 delta carotid artery sections were analyzed by IHC for total IRE1a. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0212235) licensed under a CC-BY license.")
![<b>Genetic Strategies Validation. </b>Western Blot: IRE1 alpha Antibody [NB100-2324] - Total IRE1 Alpha protein in lysates from Min6 cells which were transfected with GFP-siRNA or Ire1-siRNA. Theoretical molecular weight: 110 kDa.](http://images.novusbio.com/fullsize/IRE1-alpha-Antibody-Western-Blot-NB100-2324-img0006.jpg)
![Western Blot: IRE1 alpha Antibody [NB100-2324] - ALOX15 knockout blocks alcohol-induced up-regulation of IRE1a in mouse liver. Image from verified customer review.](http://images.novusbio.com/fullsize/IRE1-alpha-Antibody-Western-Blot-NB100-2324-img0009.jpg)
![Immunocytochemistry/Immunofluorescence: IRE1 alpha Antibody [NB100-2324] - IRE-1 alpha antibody was tested in HeLa cells at 1:200 against Dylight 488 (Green). Alpha tubulin and nuclei were counterstained against Dylight 568 (Red) and DAPI (Blue).](http://images.novusbio.com/fullsize/IRE1-alpha-Antibody-Immunocytochemistry-Immunofluorescence-NB100-2324-img0005.jpg)
![Immunohistochemistry-Paraffin: IRE1 alpha Antibody [NB100-2324] - Analysis of a formalin fixed mouse colon tissue section using total IRE1 alpha antibody (NB100-2324) at 1:300. Note a strong cytoplasmic signal in various cells of colonic villi (columnar epithelial and goblet cells) and the muscular layer. A few cells, potentially with active UPR, showed nuclear positivity also while the signal was negligible in cells at base of crypts and lamina propria.](http://images.novusbio.com/fullsize/IRE1-alpha-Antibody-Immunohistochemistry-Paraffin-NB100-2324-img0007.jpg)
![Immunohistochemistry-Paraffin: IRE1 alpha Antibody [NB100-2324] - Analysis of a formalin fixed mouse colon tissue section using total IRE1 alpha antibody (NB100-2324) at 1:300. Note a strong cytoplasmic signal in various cells of colonic villi (columnar epithelial and goblet cells) and the muscular layer. Some cells, most likely with active UPR, depicted nuclear positivity also while the signal was negligible in crypts cells and lamina propria.](http://images.novusbio.com/fullsize/IRE1-alpha-Antibody-Immunohistochemistry-Paraffin-NB100-2324-img0008.jpg)
![Western Blot: IRE1 alpha Antibody [NB100-2324] - Zn (II)-curc induces endoplasmic reticulum (ER) stress in mutant p53H273-carrying cells. (a) Representative photomicrographs of ER-Red Fluorescence staining in U373 cells untreated (Mock) or treated with Zn (II)-curc (100 µg/mL) for 16 h (Original magnification: 40×). (b) Quantization of ER content in U373 cells from ER-Red Fluorescence-stained cells. Mean fluorescence intensity (MFI) of each individual cell was normalized to cell size & expressed as fold-change compared with untreated cells at the same time point. Histograms represent the mean ± SD of three independent experiments. * p ≤ 0.05. (c) Western blot analysis of p53, BiP, total (tot) IRE1 alpha , phosphorylated (p) IRE1 alpha , & XBP1 spliced (s) protein levels evaluated in U373 & HT29 cells untreated or treated with Zn (II)-curc (100 µg/mL) for 24 h. (d) Densitometric analysis was performed using Image J software to calculate the ratio of the protein levels, as detected in (c), vs. beta -actin. Histograms represent the mean ± SD of three independent experiments. * p ≤ 0.05. (e) Total mRNA was extracted from U373 & HT29 cells untreated or treated with Zn (II)-curc (100 µg/mL) for 24 h. Spliced (s) Xbp1 gene expression was assayed by the polymerase chain reaction (PCR) of reverse-transcribed cDNA. Densitometric analysis was performed using Image J software to calculate the Xbp1s/28S ratio. Histograms represent the mean ± SD of three independent experiments. * p ≤ 0.05. (f) p53 gene expression was assayed by PCR as in (e). The p53/28S ratio is indicated. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32138264), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2324_rabbit-polyclonal-ire1-alpha-antibody-31020241554542.jpg)
![Immunohistochemistry: RGS2 Antibody [NBP3-10554] - Immunohistochemical analysis of spleen.](http://images.novusbio.com/fullsize/RGS2-Antibody-Immunohistochemistry-NBP3-10554-img0001.jpg "Immunohistochemistry: RGS2 Antibody [NBP3-10554] - Immunohistochemical analysis of spleen.")
![Immunocytochemistry/Immunofluorescence: RGS2 Antibody [NBP2-55551] - Staining of human cell line U-2 OS shows localization to cytosol. Antibody staining is shown in green.](http://images.novusbio.com/fullsize/RGS2-Antibody-Immunocytochemistry-Immunofluorescence-NBP2-55551-img0001.jpg "Immunocytochemistry/Immunofluorescence: RGS2 Antibody [NBP2-55551] - Staining of human cell line U-2 OS shows localization to cytosol. Antibody staining is shown in green.")
![Western Blot: RGS2 Overexpression Lysate (Adult Normal) [NBL1-15327] Left-Empty vector transfected control cell lysate (HEK293 cell lysate); Right -Over-expression Lysate for RGS2.](http://images.novusbio.com/fullsize/RGS2-Overexpression-Lysate-Adult-Normal-Western-Blot-NBL1-15327-img0002.jpg "Western Blot: RGS2 Overexpression Lysate (Adult Normal) [NBL1-15327] Left-Empty vector transfected control cell lysate (HEK293 cell lysate); Right -Over-expression Lysate for RGS2.")