GAPDH: Novus Biologicals

NB300-221

GAPDH Antibody (1D4) - BSA Free

(19 Reviews)

(455 Publications)

0.1 ml

NB300-221

Analysis of GAPDH in human nucleus pulposus cell culture (40ug/lane) using anti-GAPDH antibody. LI-COR Odyssey imaging system was used for detection. Western blot image submitted by a verified customer review.

Analysis of of HeLa cells stained with GAPDH antibody, dilution 1:100 (Green). DAPI staining of nuclear DNA (Blue). The GAPDH antibody produces strong cytoplasmic staining of healthy cells.

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.

Human eye cell lysate. Antibody used at 1:500. WB image submitted by a verified customer review.

Analysis of GAPDH in chicken pectoralis major using anti-GAPDH antibody. The primary antibody was used at a dilution of 1:4000, incubated for 1 hour at room temperature. Western blot image submitted by a verified customer review.

<b>Biological Strategies Validation. </b>GAPDH-Antibody-1D4-Western-Blot-NB300-221-img0015.jpg

<b>Biological Strategies Validation. </b>GAPDH-Antibody-1D4-Western-Blot-NB300-221-img0014.jpg

SH-SY5Y cells stained with GAPDH antibody NB300-221 (green). Nuclear DNA is stained with Hoechst dye (blue).

Lane view shows a specific band for GAPDH using 0.05 mg/mL Jurkat and MCF-7 cell lysates and antibody at 1:25. Electropherogram image of corresponding Simple Western lanes view at WES molecular weight of 40 kDa. Image reported by internal validation.

Knockdown of Ift88 or Kif3a in NP cells does not affect hyperosmotic upregulation of TonEBP. (a) TonEBP/Nfat5 mRNA levels in NP cells with Ift88 knockdown (n ≥ 5). (b) Western blot image showing increased TonEBP expression in response to hyperosmolarity (550 mOsm/kg H2O) independently of Ift88 knockdown. (c) Densitometry analyses of TonEBP with Ift88 knockdown (n ≥ 4). (d) TonEBP/Nfat5 mRNA levels in NP cells with Kif3a knockdown (n ≥ 3). (e) Western blot image showing that hyperosmotic induction of TonEBP is maintained after Kif3a knockdown. (f) Densitometry analyses of TonEBP after Kif3a knockdown (n ≥ 4). Data are represented as scatter plots (mean ± SEM). ns = not significant. One-way ANOVA or Kruskal-Wallis test with Sidak’s or Dunn’s multiple comparison test was used based on the distribution of the data to determine statistical significance. Western blot images were cropped & acquired under same experimental conditions. See Supplementary Fig. S1-1 for un-cropped Western blot images. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31664118), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - OPN induces EndoMT. (E) VE-cadherin, Tie1, Tie2, CD31, alpha -SMA, & fibronectin levels in HUVECs pre-incubated 16 h with 2% FBS-containing medium & then treated 24 h with PBS or 0.3 μg/ml of OPN. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29435158), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - miR-21-5p delivery by H-EV treatment promote NSCLC cell proliferation, survival & mobility by targeting PTEN, PDCD4 & RECK. a–d, western blot detecting PTEN, PDCD4 & RECK protein expression level in A549 or H23 cells after different treatment as described in Fig. 4. e–k, cell functional assay as described in Fig. 1. A549 or H23 cells with or without PTEN, PDCD4 or RECK gene overexpression (O/E) were tested. Wild type, non-treated A549 or H23 cells were used as negative control (NC). Bar in K indicates 20 μm. Tukey’s test was used for statistical analysis. *, p < 0.05; **, p < 0.01; ***, p < 0.001; ****, p < 0.0001 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30736829), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - Expression of CTGF & TGF‐ beta 1 in WT & MMP‐13 KO mice treated without & with NDMA. (A) Real‐time PCR analysis for the quantitative expression of CTGF, TGF‐ beta 1, alpha ‐SMA & collagen type 1 mRNA in WT & MMP‐13 KO mice. The data are mean ± S.D. of six samples per group. ***P < 0.001 NDMA‐treated WT mice versus control untreated WT mice; *P < 0.05 NDMA‐treated MMP‐13 KO mice versus untreated MMP‐13 KO mice; #P < 0.001 NDMA‐treated MMP‐13 KO mice versus NDMA‐treated WT mice. (B) Semiquantitative RT‐PCR for the expression of CTGF, TGF‐ beta 1, alpha ‐SMA & type 1 collagen mRNA in WT & MMP‐13 KO mice treated without & with NDMA. GAPDH was used as a loading control. The data are representative of six samples in each group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28782260), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - Hydrogen sulfide donors leads to inhibition of phosphate transport. Cells were cultured in a normal or calcific environment exposed to AP72 (20 μmol·L−1) for 5 days. (a) Phosphate content was determined using QuantiChrom quantitative colorimetric assay. (b) Pit1 & (c) Pit2 western blotting was performed & normalized to GAPDH. Data shown are means ± SEM of five independent experiments. *P < .05, significantly different as indicated; ns, not significant Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31017307), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - Overexpression of NICD increases the total Fmod protein contents in BMDMs & LPS prevents the cleavage of Fmod in a dose dependent manner. (A,B) WB shows the expression of total Fmod in Apoe−/− & Notch1+/−;Apoe−/− BMDMs & quantification of three replicates as determined by Image J. (C,D) WB showing the total Fmod protein content in WT BMDMs 48 h post transfection with empty or NICD plasmids & the quantification of the immunoblots. (E,F) qRT-PCR showing the panel of M1 & M2 genes dysregulated with human recombinant FMOD (400 ng/ml for 24 h). (G) Co-immunoprecipitation showing contents of Tgf-beta 2, Fmod & NICD proteins pulled down with Fmod antibody from the WT & Notch1+/− peritoneal macrophages. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31142802), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - Lactate dehydrogenase (LDH) assay & the Western blot of kidney injury molecule (KIM)-1 & N-cadherin in rat mesangial cells (RMCs). Cells were treated with bicalutamide (Bic) at concentrations of 30 & 60 μM at 24 h. (a) LDH release was increased by Bic (n = 3, * p < 0.05). (b) A representative blot of protein expressions of KIM-1 & N-cadherin. GAPDH was used as an internal control. (c) Quantitative data of Western blotting of KIM-1(n = 3, * p < 0.05). (d) Quantitative data of Western blotting of N-cadherin (n = 3, * p < 0.05). When RMCs were treated with Bic, N-cadherin dose-dependently decreased, however KIM-1 was significantly induced in the group treated with 60 μM. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32403414), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - Immediate early gene (IEG) expression in RICH2 KO mice. IEG expression was analyzed in nuclear protein lysate from amygdala & normalized to GAPDH levels. No significant difference was detected in the expression of (A) activity-regulated cytoskeleton-associated protein (ARC; Unpaired t-test, n = 3, p = 0.077), & (B) c-FOS (Unpaired t-test, n = 3, p = 0.8784). A significant difference was detected in the expression of (C) cyclic AMP response element-binding protein (CREB; Unpaired t-test, n = 3, p = 0.002). The amount of phosphorylated CREB (pCREB) was unchanged (Unpaired t-test, n = 3, p = 0.1822). Exemplary Western blot bands are shown. Histone H3 was used a control for the presence of nuclear proteins in the lysate. Image collected & cropped by CiteAb from the following publication (//journal.frontiersin.org/article/10.3389/fnmol.2017.00180/full), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - Relative Myonectin/CTRP15 content.Relative Myonectin/CTRP15 content was examined in the rat diaphragm muscle of the male lean zucker (LZR) & obese zucker rats (OZR). Exercised animals were trained on a motorized treadmill for 9 wk. Control animals were exposed to the similar environment (positioned next to the treadmill) but were not exercised. (A) Shows representative western blots for Myonectin & GAPDH. (B) The data are expressed in arbitrary units with values normalized to mean control value within phenotype. Image collected & cropped by CiteAb from the following publication (//peerj.com/articles/605), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - FerrylHb induces HO-1 & ferritin in EC. Confluent HUVECs grown on 6-well plates were exposed to heme, Hb, metHb, & ferrylHb (100 μmol/L heme or as indicated in complete medium containing 15% of FBS). After 4 hours of incubation total RNA was isolated & HO-1 mRNA level was measured by quantitative RT-PCR (panels (a) & (d)). For protein expression, HUVECs were solubilized after 8 hours of treatment. HO-1 & ferritin H & L expression was detected by Western blot ((b) & (e)) or with ELISA (c). Immunoblots were reprobed with GAPDH & are representative of three independent experiments. Results are shown as mean ± S.D. (n = 3) from one representative experiment of three. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23766856), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - microRNA-200c regulates MARCKS.(A) The effect of miR-200c transfection on mRNA levels of predicted target genes in Wm266.4 melanoma cells was assessed using GAPDH as a control. Lower panel: immunoblot of MARCKS expression. (B) Brightfield imaging & morphological quantification of Wm266.4 cells transfected with siRNAs targeting miR-200c-responsive genes. (C) MARCKS knock-down by four individual siRNAs leads to rounded cell shape in Wm266.4 cells. (D) Levels of MARCKS mRNA in melanoma cell lines & normal melanocytes, measured by qPCR & normalized to levels of GAPDH. Error bars represent ± SEM; unpaired t-test *p<0.05 **p<0.01. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/20957176), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - Dose-dependent effects of LPS/IFN-gamma on Tgf-beta expression are associated with changes in the cleaved Fmod fragments. (A) Representative WB image showing the contents of NICD, Mmp8, total Fmod, cleaved Fmod, Tgf-beta 2 & Gapdh in macrophages in response to increasing dose of LPS (0, 5, 10, 25, 50 or 100 ng/ml) for 24 h. (B–F) Quantitation of immunoblots for NICD, Mmp8, total Fmod, cleaved Fmod, Tgf-beta 2 respectively (average of three replicates shown after normalizing the intensity with Gapdh. (WB = Western blot). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31142802), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - OPN induces EndoMT. (C) mRNA levels of VE-cadherin, Tie1, Tie2, CD31, alpha -SMA, & fibronectin in HUVECs pre-incubated 16 h with 2% FBS-containing medium & then treated 15 h with PBS or 0.3 μg/ml of OPN. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29435158), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - miR-200a associated elongation is associated with decreased actomyosin contractility.(A) The effect of miR-200a transfection on mRNA levels was measured for predicted target genes in Wm266.4 melanoma cells using GAPDH as a control. (B) Transfection of Wm266.4 cells with miR-200a leads to decreased pMLC levels. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/20957176), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - Regulation of cell migration-associated proteins by NCKU-21 in A549 & CL1-5 cells.Protein expressions of matrix metalloproteinase-2 (MMP-2) & MMP-9 were analyzed in A549 (A) & CL1-5 (B) cells treated with NCKU-21 for 24 hr. * P < 0.05 & ** P < 0.01, compared to the control group (without NCKU-21 treatment). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28945763), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - TNF alpha negatively regulates EC differentiation: the effect of TNF alpha on VEGF-A-stimulated differentiation of MSCs into ECs was examined. TNF alpha R & VEGFR-2 mRNA expression was analyzed by RT-PCR (n = 3) (a). Sox18 protein levels were measured by Western blot analysis (n = 3) (b). Expression of EC markers was determined by FACS analysis, & a representative grid is shown (n = 3-4) ((c)–(g)). Endothelial tube formation was examined using an angiogenesis assay (n = 3) ((d)–(h)). Experiments were performed with samples taken from independent BM-MSC cultures from separate microswine. HUVECs were excluded from statistical analyses. Data are shown as mean ± SD. ∗p < 0.05 versus naïve MSCs & #p < 0.05 MSCs treated with VEGF-A versus VEGF-A plus TNF alpha cotreatment. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26106428), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - RICH2 is expressed at glutamatergic synapses in the amygdala. (A) Expression of Rich2 was detected on mRNA level using a PCR approach in amygdala using lysate from wild type (WT) mice. Cortex lysate was used as control as expression of Rich2 has been reported in cortex previously. The expression levels of Rich2 in amygdala were slightly higher compared to cortex. The primers used for amplification of Rich2 were placed in a region deleted in the genome of RICH2 Knockout (KO) mice. Absence of Rich2 expression in amygdala of RICH2 KO mice was confirmed. (B)In situ hybridization confirms Rich2 expression in the amygdala in adult WT animals. (C) RICH2 protein was not detected in RICH2 KO mice, but in amygdala of WT mice, & hippocampus & cortex as reported previously. ARP1 is a protein enriched in amygdala & was used as control to ensure proper preparation of amygdala tissue. (D) Immunocytochemistry performed on brain sections of WT mice reveals RICH2 signals co-localizing with HOMER1, a marker for excitatory postsynapses, in the amygdala. Top left: overview indicating magnified area in bottom left & right images. Arrows indicate clearly co-localizing signals (scale bar = 20 μm). Image collected & cropped by CiteAb from the following publication (//journal.frontiersin.org/article/10.3389/fnmol.2017.00180/full), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - The absence of primary cilia in Kif3a null MEFs has a small effect on hyperosmotic induction of TonEBP without influencing its TAD activity (a) TonEBP/Nfat5 gene expression in wild-type & Kif3a null (Kif3a−/−) MEFs under hyper- (600 mOsm/kg H2O) & hypoosmotic (200 mOsm/kg H2O) conditions. (b,c) Western blot image & corresponding densitometry analyses showing TonEBP levels under different osmotic conditions in wild-type & Kif3a null MEFs. Kif3a null MEFs show slightly attenuated hyperosmotic increase but unaffected hypoosmotic decrease in TonEBP expression. (d,e) TonEBP-TAD (Ton-TAD) activity in wild-type & Kif3a null MEFs under hyperosmotic (d) & hypoosmotic (e) conditions (n = 4). Similar to wild-type cells, Kif3a null MEFs show increase & decrease in TonEBP-TAD activity under hyperosmotic & hypoosmotic conditions, respectively (n ≥ 3 with 3 technical replicates per biological replicate). Data are represented as scatter plots (mean ± SEM). ns = not significant. One-way ANOVA or Kruskal-Wallis test with Sidak’s or Dunn’s multiple comparison test was used based on the distribution of the data to determine statistical significance. Western blot images were cropped & acquired under same experimental conditions. See Supplementary Figs S1 & 3 for un-cropped Western blot images. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31664118), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - Inhibition of AKT/GSK3 beta / beta -catenin signaling pathway decreased HMGB1-induced EMT.(a) BEAS-2B cells treated w/ 10 μM PI3K inhibitor (LY294002) & GSK-3 beta inhibitor (SB415286) for 10 min, & then treated w/ HMGB1 (300 ng/mL) for 24 h. Protein expression detected by WB analysis. Quantification of E-cadherin, ZO-1, & vimentin performed using ImageJ software. Data are expressed as mean ± SD (n = 5). #p < 0.05, as compared w/ control group. *p < 0.05, as compared w/ HMGB1-treated group. (b) BEAS-2B cells transduced w/ lentiviral-expressed beta -catenin shRNA (1 MOI) for 72 h & selected by puromycin. The mRNA from stable clones expressing beta -catenin-targeting shRNAs analyzed by quantitative real-time PCR. Data are expressed as mean ± SD (n = 5). ##p < 0.01, ###p < 0.001, as compared w/ control group. **p < 0.01, ***p < 0.001, as compared w/ vector group. (c) beta -catenin protein expression detected by WB analysis in a stable beta -catenin shRNA BEAS-2B cell clone. Quantification of protein expression performed using ImageJ software. Data are expressed as mean ± SD (n = 3). ##p < 0.01, ###p < 0.001, as compared w/ control group. **p < 0.01, ***p < 0.001, as compared w/ vector group. (d) A stable beta -catenin shRNA BEAS-2B cell clone treated w/ HMGB1 (300 ng/mL) for 24 h, & protein expression of E-cadherin, ZO-1, & vimentin detected by WB analysis. Quantification of protein expression performed using ImageJ software. Data are expressed as mean ± SD (n = 4). #p < 0.05, as compared w/ control group. *p < 0.05, as compared w/ HMGB1 group. In immunoblotting assay, gels have been run under the same experimental conditions. Then cropped blots incubated w/ different primary antibodies for analysis of signaling pathway. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26739898), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - Ang II counteracts IL-6 or TNF alpha inhibition of EC differentiation: the combined effects of Ang II, IL-6, & TNF alpha on VEGF-A-stimulated differentiation of MSCs into ECs were examined. TNF alpha R, IL-6R, AT2R, & VEGFR-2 mRNA expression was analyzed by RT-PCR (n = 3) (a). Sox18 protein levels were measured by Western blot analysis (n = 3) (b). Expression of EC markers was determined by FACS analysis, & a representative grid is shown (n = 3-4) ((c)–(h)). Endothelial tube formation was examined using an angiogenesis assay (n = 3) ((d)–(i)). Experiments were performed with samples taken from independent BM-MSC cultures from separate microswine. HUVECs were excluded from statistical analyses. Data are shown as mean ± SD. ∗p < 0.05 versus naïve MSCs, #p < 0.05 MSCs treated with VEGF-A versus VEGF-A plus Ang II cotreatment, & alpha p < 0.05 versus MSCs treated with VEGF-A & Ang II versus VEGF-A & Ang II plus IL-6 and/or TNF alpha . Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26106428), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - HMGB1-activated AKT/GSK3 beta / beta -catenin signaling pathways.(a) BEAS-2B cells were treated with different doses of HMGB1 for 10 min & expression of different proteins was detected by western blot. (b) BEAS-2B cells were treated with HMGB1 (300 ng/mL) for different periods & analyzed for expression of different proteins by western blot. (c) BEAS-2B cells were treated with HMGB1 (300 ng/mL) for different periods & analyzed for beta -catenin expression by western blot. (d) BEAS-2B cells were treated with HMGB1 (300 ng/mL) for different periods & analyzed for beta -catenin mRNA expression by real-time quantitative PCR. (e) BEAS-2B cells were treated with HMGB1 (300 ng/mL) for different periods & analyzed for nuclear & cytosolic beta -catenin expression by western blot. (f) BEAS-2B cells were treated with 10 μM PI3K inhibitor (LY294002) & GSK-3 beta inhibitor (SB415286) for 10 min, & then treated with HMGB1 (300 ng/mL) for 24 h. beta -catenin expression was assessed by western blot analysis. Quantification of protein expression was performed using ImageJ software. Data are expressed as mean ± SD. *p < 0.05, **p < 0.01, as compared with the control group. #p < 0.05, as compared the HMGB1-treatment group. (A,B) (n = 4); (C–F) (n = 3). (g) Immunofluorescence staining of beta -catenin (green) was detected by fluorescence microscopy. Data are expressed as mean ± SD (n = 4). *p < 0.05, as compared with the 0-min group. In immunoblotting assay, gels have been run under the same experimental conditions. Then cropped blots were incubated with different primary antibodies for analysis of signaling pathway. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26739898), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - Silencing of endogenous VEGF-A lacks an effect on mesenchymal stem cell differentiation into endothelial cells. Differentiating mesenchymal stem cells (MSCs) were transfected with small interfering RNA (siRNA) directed against vascular endothelial growth factor (VEGF-A) & then examined for endothelial cell (EC) marker expression. Treatment of MSCs with the cocktail of VEGF-A (2 ng/ml) plus angiotensin II (Ang II; 2 ng/ml) for 24 hours induced a synergistic increase in VEGF transcript as compared with VEGF-A alone or Ang II alone (A). VEGF-A mRNA was normalized to glyceraldehyde-3-phosphate dehydrogenase (GAPDH) mRNA (A). Standardization experiments demonstrated that 50 nM siRNA directed against VEGF completely abrogated VEGF protein expression (B). Fluorescence-activated cell sorting analysis revealed that there was no significant difference in EC marker expression between differentiating MSCs that received VEGF-A siRNA or scrambled control siRNA (C, D, E). Note that human umbilical vein endothelial cells (HUVECs) were excluded from the statistical analyses. *P <0.05 vs. naïve MSCs. #P <0.05 vs. VEGF-A (2 ng/ml)-treated MSCs or Ang II (2 ng/ml)-treated MSCs alone, n = 3. Image collected & cropped by CiteAb from the following publication (//stemcellres.biomedcentral.com/articles/10.1186/scrt538), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - N-EV & H-EV treatment promote macrophage M2 polarization by delivering miR-21-5p that targets PTEN. a, western blot analysis of PTEN protein expression level in induced macrophages. H/i-miR-EV, monocytes were induced with the presence of EV secreted by miR-21-5p-inhibited, hypoxia pre-challenged MSCs; H-EV + i-miR, monocytes were transfected with miR-21-5p inhibitor-expressing vector before induction with the presence of H-EV. Macrophages induced without MSC-EV were used as negative control (NC). b, c, flow cytometry determining the percentage of CD163+CD206+ cells among total CD68+ cells after induction. N-EV + O/E PTEN or H-EV + O/E PTEN, monocytes were transfected with PTEN overexpressing vector before N-EV or H-EV treatment, respectively. d–f, western blot detecting Akt & STAT3 protein expression as well as their activating phosphorylation (p-Ser473 for Akt & p-tyr705 for STAT3) in macrophages after induction. g–i, ELISA evaluating IL-10, TGF-beta & VEGF-alpha in macrophage culture medium after induction. Macrophages induced with the presence of N-EV were used as negative control in b–i. Tukey’s test was used for statistical analysis. *, p < 0.05; **, p < 0.01; ***, p < 0.001; ****, p < 0.0001 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30736829), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Western Blot: GAPDH Antibody (1D4) [NB300-221] - Demonstration of the advantages of crude fractionation over whole cell lysis & scale up of the approach. (A) HEK293 cells were plated at a density of 4 × 105 cells per well of a 12 well plate & subsequently lysed directly in NP40 or RIPA lysis buffer or processed according to the protocol in Figure 2 (Sequential). An aliquot of each extract was then analyzed by 4-12% SDS PAGE followed by staining with Coomassie blue or by Western blotting & probing with antibodies to various marker proteins of specific intracellular organelles as previously. (B) HEK293 cells were plated at a density of 4 × 105 cells per well of a 12 well dish & then transfected the next day in triplicate with 400 ng of a construct encoding V5/6×-HIS tagged ERGIC-53. Cells were extracted 48 hours later either directly in RIPA buffer, directly in NP40 buffer or according to our extraction protocol. Proteins were then partially purified from each extract using Nickel resin (SIGMA #P6611) & eluted proteins were analyzed by 10% SDS PAGE followed by staining with Coomassie blue or by Western blotting & probing with the anti V5 antibody. (C) HEK293 cells were plated at a density of 4 × 105 cells per well of a 12 well dish & then transfected the next day in with 1600 ng of pcDNA6/V5-His (Invitrogen) or constructs encoding WT or MUT COMP. Cells were harvested 48 hours later & extracted according to our protocol. (D) HEK293 cells were plated at a density of 4 × 105 cells per well of a 12 well dish or 8.4 × 105 cells per well of a 35 mm dish & processed according to the protocol in Figure 2. An aliquot of each extract was then analyzed by 4-12% SDS PAGE followed by Western blotting & probing with antibodies to GAPDH, BiP & Lamin A. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/20003239), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

$Western Blot: GAPDH Antibody (1D4) [NB300-221] - Notch1, ApoER2 & Dab1 colocalize in hippocampal neurons. (A) Representative image of fluorescent immunolabeling shows that Notch1 is localized in a subset of CA3 neurons, co-expressing Dab1 & ApoER2 (magnified insert). ApoER2 is highly expressed in all CA3 neurons. (B) Fluorescent immunolabeling shows the distribution of Notch1 & Dab1 as compared to Arc/Arg3.1 in CA3 neurons. (B′) Close up of a dendrite showing colocalization of the three proteins (white arrowheads). (C) Western blot analysis on immunoprecipitated samples from whole hippocampal lysate shows that Notch1 displays a strong interaction with Dab1 whereas Notch1 & ApoER2 interaction appears weaker in the preparation (n = 4 independent experiments). (D) Immunolabeling on immunoprecipitated samples from whole cortical lysates show that Notch1 & Dab1 interact. ApoER2 is bound to both Notch1 & Dab1 (n = 3 independent experiments). (E) Co-IP from synaptosomal membrane fractions reveals a stronger interaction between Notch1 & ApoER2, which is reduced in the N1cKO (n = 3 independent pulldowns). In (C–E) GAPDH is used as a loading control for the inputs & to detect contamination in the IP samples. Scale bar in (A) is 50 μm & (B) 25 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26635527), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

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.

$Western Blot: GAPDH Antibody (1D4) [NB300-221] - Analysis of GFAP in mouse models of AxD by immunoblotting.Urea-soluble fractions extracted from wild type (GFAP+/+), R236H mutant knockin (GFAPR236H/+) & human wild type GFAP transgenic (GFAPTg) mice (n = 3 for each genotype) were analyzed by immunoblotting with indicated anti-GFAP antibodies (A-D). Immunoblots were also probed with antibodies specific to alpha B-crystallin (F) & GAPDH (E), which was used as a loading control. Representative images were shown, with the antibody used for immunoblotting was indicated above each panel. Approximate molecular weight markers (in kDa) were shown on the right. Dashed lines indicated lanes that samples run on the same gel but were noncontiguous (D & F). Notice that although all anti-GFAP antibodies tested recognized full-length GFAP (A-D), both 2.2B10 (A) & SMI-21 (B) antibodies also detected GFAP degradation products sized between 25 & 35 kDa in GFAPTg mice. The level of alpha B-crystallin (F) was increased in both GFAPR236H/+ & GFAPTg mice compared to wild type controls (GFAP+/+). Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0180694), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: GAPDH Antibody (1D4) [NB300-221] - Knockdown of Ift88 or Kif3a in NP cells does not affect hyperosmotic upregulation of TonEBP. (a) TonEBP/Nfat5 mRNA levels in NP cells with Ift88 knockdown (n ≥ 5). (b) Western blot image showing increased TonEBP expression in response to hyperosmolarity (550 mOsm/kg H2O) independently of Ift88 knockdown. (c) Densitometry analyses of TonEBP with Ift88 knockdown (n ≥ 4). (d) TonEBP/Nfat5 mRNA levels in NP cells with Kif3a knockdown (n ≥ 3). (e) Western blot image showing that hyperosmotic induction of TonEBP is maintained after Kif3a knockdown. (f) Densitometry analyses of TonEBP after Kif3a knockdown (n ≥ 4). Data are represented as scatter plots (mean ± SEM). ns = not significant. One-way ANOVA or Kruskal-Wallis test with Sidak’s or Dunn’s multiple comparison test was used based on the distribution of the data to determine statistical significance. Western blot images were cropped & acquired under same experimental conditions. See Supplementary Fig. S1-1 for un-cropped Western blot images. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31664118), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - S166 phosphorylation facilitates necrosome formation.a BMDMs from mice of the indicated genotypes were treated with TNF (T; 10 ng ml−1), SMAC mimetic (S (Birinapant); 1 µM) & Z-VAD-FMK (Z) for 0, 2 & 4 h. RIPK1 immunoprecipitates & total cell lysates (input) were analyzed by immunoblotting with the indicated antibodies. b BMDMs from mice of the indicated genotypes were treated with TNF (T; 10 ng ml−1), SMAC mimetic (S (Birinapant); 1 µM) & Z-VAD-FMK (Z) for 2 & 4 h. Lysates were processed under non-reducing conditions & analyzed for presence of MLKL by immunoblot. c BMDMs from mice of the indicated genotypes were treated with LPS (L; 100 ng ml−1) & Z- VAD-FMK (Z) for 13 & 15 h. Lysates were processed under non-reducing or reducing conditions & analyzed by immunoblot using the indicated antibodies. d BMDMs from mice of the indicated genotypes were treated with Poly(I:C) (P; 0.5 μg ml−1) & Z-VAD-FMK (Z) for 13 & 15 h. Lysates were processed under non-reducing or reducing conditions & analyzed by immunoblot using the indicated antibodies. a, c Representative data of three independent experiments is shown. b, d Representative data of two independent experiments is shown. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32269263), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - Notch1 affects CREB phosphorylation & transcription. (A) Immunoblot on whole hippocampal lysates shows a substantial reduction in CamKII in hippocampi of N1cKO as compared to WT. beta -actin is used as a loading control (n = 3 independent experiments). (B) Quantification of CamKII protein expression between N1cKO & WT normalized to beta -actin shows a reduction by 78% in N1cKO hippocampi (n = 6 animals per genotype; Student’s t-test, p < 0.05). (C) Western blot on hippocampal lysates shows ERK1/2 phosphorylation (pERK1/2) in N1cKO is reduced as compared to WT hippocampi. beta -actin is used as a loading control (n = 3 independent experiments). (D) Quantification of ERK1/2 phosphorylation in N1cKO as compared to WT indicates a 76% decrease in KO samples (n = 6 mice per genotype; Student’s t-test, p < 0.05). (E) Immunoblot on whole hippocampal lysates shows a reduction in CREB phosphorylation in N1cKO as compared to WT (n = 3 independent experiments). (F) Bar graph shows a near to significance 56% reduction in CREB phosphorylation in N1cKO hippocampi as compared to WT (n = 4 animals per genotype; Student’s t-test, p = 0.069). (G) Graph summarizing transcripts expression of CREB targets, Egr1, Bdnf & c-fos, in hippocampi from cage control (CC) & environmental exposed (EE) WT & N1cKO mice (n = 3–4 mice per genotype; Student’s t-test, p < 0.05; Black bars compare WT CC w/ WT EE; gray bars compare WT EE w/ N1cKO EE). (H) Model of proposed Notch1 non-canonical signaling regulations of Reelin, NMDA & CREB pathways described in this study. Elements putatively connecting Notch1/Reelin signaling to Notch1/Glutamaterigic signaling are dotted & are based on existing literature. Data are averages ± SEM & *=p < 0.05; 0 signifies p = 0.5. Image collected & cropped by CiteAb from following publication (//pubmed.ncbi.nlm.nih.gov/26635527), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - Altered Rho GTPase signaling in amygdala of RICH2 KO mice. (A) Comparison between the GTPase activating protein (GAP) activity of the P2 lysates from WT & RICH2 KO mice. The GAP activity is measured in nmoles/min/mg of small G-protein. First a standard curve is made using the absorbance of KH2PO4 at different concentrations, later the absorbance of WT & RICH2 KO lysates are plotted on the graph. The GAP activity is higher for WT lysates compared to RICH2 KO lysates. (B) In the presence of the small G protein RhoA, the absorbance of WT lysates is higher than that of RICH2 KO lysate, which indicates that RICH2 is acting as a GAP for RhoA in amygdala. (C) There is no difference between the absorbance of WT & RICH2 KO lysates in the presence of RAC1 & CDC42 (D,E) Like RAC1 & CDC42, RAS p21 is not a target G protein for RICH2 in amygdala as there is no difference in the absorbance of WT & RICH2 KO lysates in the presence of RAS p21. (F) Western blot analysis of amygdala P2 lysates reveals that expression of RhoA is significantly higher in RICH2 KO lysates, in comparison with WT lysates (Unpaired t-test, p = 0.0508, n = 3). (G,H) Western blot analysis revealed no alteration in the expressions of Rac1 (G) & Cdc42 (H) between WT & RICH2 KO using amygdala P2 lysates. Image collected & cropped by CiteAb from the following publication (//journal.frontiersin.org/article/10.3389/fnmol.2017.00180/full), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

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.

$Western Blot: GAPDH Antibody (1D4) [NB300-221] - Optimization of digitonin concentration for the extraction of cytosolic proteins. (A) HEK293 cells were plated at a density of 4 × 105 cells per well of a 12 well plate & were harvested 48 hours later. Cells were then lysed in 400 μl of buffer containing digitonin at the concentration indicated. Following centrifugation & collection of the supernatant the remaining cell pellet was further extracted in NP40 lysis buffer. An aliquot of each extract was then analysed by 4-12% SDS PAGE (Invitrogen #NP0322) followed by staining with Coomassie blue. (B) The concentration of protein in each extract was determined by colorimetric protein assay (Pierce #23232) & the results were plotted to demonstrate that total protein extracted was the same regardless of the starting concentration of digitonin. (C) Extracted proteins from each fraction were analyzed by Western blot using an anti GAPDH antibody (NOVUS Biologicals #300-221B) as a marker of the cytosol & an anti BiP antibody (SIGMA # G918) as a marker of the endoplasmic reticulum. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/20003239), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: GAPDH Antibody (1D4) [NB300-221] - CCL2 promotes prostate cancer cell migration & induces CCL22 secretion, which is a ligand of CCR4A. Prostate cancer cells are placed in transwell inserts & treated with CCL2 (0–30 ng/ml). After 24-h incubation, PC-3 & DU145 cells that had migrated through the membrane are stained. The mean OD value is read using a microreader at 595 nm. Migration of LNCaP cells is assessed with a wound-healing assay. Data are presented as mean ± SD. B. DU145 cells are co-cultured with THP-1 & U937 cells & treated with CCL2 (30 ng/ml) for 24 h, CM is collected, & CCL17 & CCL22 levels are analyzed using ELISA. The mean OD value is read using a microreader at 450 nm, & data are presented as mean ± SD. C, D. Total RNA & protein are extracted from prostate cancer cells, & CCR2 & CCR4 gene & protein expression levels are analyzed using PCR (C) & western blot (D). E. Prostate cancer cells (1.0 × 105 cells/well) are seeded into 6-well plates & cultured until they reach 60%–70% confluence. Cells are incubated with anti-CCR2 or anti-CCR4 antibody & detected using a second antibody conjugated with FITC (green). Cells are counterstained with 4',6-diamidino-2-phenylindole (blue). Adjustments of brightness, contrast, & size are applied to the whole images of western blot-based analyses without elimination of any information present in the original, including backgrounds. All experiments are performed in triplicate, & mean values are shown. *p < 0.05, **p < 0.01, ***p < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28039457), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - Stable knockdown of Ift88 or Kif3a inhibits formation of NP cell primary cilia. (a) Ift88 mRNA levels in NP cells transduced with control (ShCtr) or two different ShIft88 clones were measured by qRT-PCR to confirm the knockdown (n ≥ 5). (b) Western blot image showing significant reduction of IFT88 protein levels after the knockdown of Ift88. (c) Densitometry analyses of Western blots confirm significant knockdown of IFT88 (n ≥ 5). (d–f) qRT-PCR, Western blot, & corresponding densitometry analyses, show significant downregulation of KIF3A after stable knockdown using two different ShKif3a clones (n ≥ 4). (g) Acetylated alpha -tubulin immunofluorescence staining after lentiviral transduction of ShIft88 or ShKif3a shows inhibition of primary cilia formation in majority of rat NP cells. Scale bar = 75 μm. White arrowheads point to primary cilia. (h,i) Quantitation of percentage of NP cells with primary cilia & primary cilium length after stable silencing of Ift88 or Kif3a (n = 3; at least 150 cells/group). Data are represented as scatter plots (mean ± SEM). ns = not significant. One-way ANOVA or Kruskal-Wallis test with Sidak’s, Holm-Sidak’s, or Dunn’s multiple comparison test was used based on the distribution of the data to determine statistical significance. For statistical comparison of the percentages of NP cells with primary cilia, Fisher’s exact test was used. Western blot images were cropped & acquired under same experimental conditions. See Supplementary Fig. S1–1 for un-cropped Western blot images. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31664118), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - CCL2 increases not only CCL22 but also CCR2 & CCR4A. Prostate cancer cells are treated with CCL2 (30 ng/ml) for 24 h, & western blot for CCR2 is performed. B. Prostate cancer cells are treated with CCL2, CCL17, & CCL22 (30 ng/ml) for 24 h, & western blot for CCR4 is performed. C. Prostate cancer cells are co-cultured with U937 or U937-M cells for 24 h, & western blot for CCR4 is performed. D. Prostate cancer cells are placed in transwell inserts & treated with CCL17 & CCL22 (0–30 ng/ml). After 24-h incubation, PC-3 & DU145 cells that had migrated through the membrane are stained. The mean optical density (OD) value is read using a microreader at 595 nm. Migration of LNCaP cells is assessed with a wound-healing assay. Adjustments of brightness, contrast, & size are applied to the whole images of western blot-based analyses without elimination of any information present in the original, including backgrounds. Data are presented as mean ± SD. All experiments are performed in triplicate, & mean values are shown. *p < 0.05, **p < 0.01, ***p < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28039457), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - ATR2 siRNA transfection & immunophenotyping for EC markers. I Concentration selection for siRNA transfection. Three different concentrations (10, 35, & 50 nM) of ATR2 siRNA were used according to the manufacturer’s protocol. Western blot analysis showed inhibition of ATR2 by 10, 35, & 50 nM of ATR2 siRNA. However, 50 nM of ATR2 siRNA showed the highest inhibition among all three different concentrations (A). ATR2 silencing by siRNA transfection with EGM compared with AMSCs with EGM & EGM + scrambled siRNA (negative control) (B). GAPDH was used as a housekeeping gene. II Flow cytometric analysis of PECAM1 (CD31) in four different groups; control group with EGM (A), AMSCs with EGM & MMP-2 siRNA (B), AMSCs with EGM & MMP-14 siRNA (C), & HUVECs as the positive control (D). Cell transfection with 5 μM of ATR2 siRNA for EGM (E), AMSCs with EGM & MMP-2 siRNA (F), & AMSCs with EGM & MMP-14 siRNA (G). Flow cytometry data were analyzed to show the significant differences between the groups (H). III Flow cytometric analysis of VE-cadherin (CD144) in four different groups: control group AMSCs with EGM (A), AMSCs with EGM & MMP-2 siRNA (B), AMSCs with EGM & MMP-14 siRNA (C), & HUVECs as the positive control (D). Cell transfection with 5 μM of ATR2 siRNA for EGM (E), AMSCs with EGM & MMP-2 siRNA (F), & AMSCs with EGM & MMP-14 siRNA (G). Flow cytometry data were analyzed to show the significant differences between the groups (H). **p < 0.01. EBM endothelial cell basal medium, EGM endothelial cell growth medium, MMP matrix metalloproteinase, ATR2 angiotensin receptor R2, HUVEC human umbilical vein endothelial cell Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28499402), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - Protein expression of CTGF, TIMP‐1, TGF‐ beta 1, alpha ‐SMA & collagen type 1 in WT & MMP‐13 KO mice treated without & with NDMA. (A) Western blotting for the proteins of full‐length CTGF & its C‐terminal fragments, TIMP‐1, active TGF‐ beta 1, alpha ‐SMA & collagen type 1 in the liver tissues from WT & MMP‐13 KO mice. The images are representative of six Western blots per each group. (B) Quantitative analysis of Western blot images. The data are mean ± S.D. of six images per group. ***P < 0.001 NDMA‐treated WT mice versus control untreated WT mice & NDMA‐treated MMP‐13 KO mice versus untreated MMP‐13 KO mice; **P < 0.01 NDMA‐treated MMP‐13 KO mice versus untreated MMP‐13 KO mice; *P < 0.05 NDMA‐treated MMP‐13 KO mice versus untreated MMP‐13 KO mice; #P < 0.001 NDMA‐treated MMP‐13 KO mice versus NDMA‐treated WT mice; @, P < 0.05 NDMA‐treated MMP‐13 KO mice versus NDMA‐treated WT mice. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28782260), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - Endothelial responses provoked by Hb-lipid interactions are attenuated by sulfide donors. (a) OxLDL (200 μg/mL) was incubated with sulfide donors NaSH, GYY4137, AP67, & AP72 at the concentrations of 20 & 200 μmol/L at 37°C for 24 hours. Confluence HAoECs were exposed to the LDL samples for 4 hours then cell viability was determined by MTT assay. Representative experiment, n = 3, each performed in 8 wells in parallel. (b) OxLDL (200 μg/mL) was incubated with sulfide donors NaSH, GYY4137, AP67, & AP72 at the concentration of 20 & 200 μmol/L at 37°C for 24 hours. Confluence HAoECs were exposed to LDL samples (50 μg/mL) for 8 hours. HO-1 & HO-2 protein expressions were determined by Western blotting. Representative experiment, n = 3. (c–e) Hb (10 μmol/L) was incubated with H2O2 (50 μmol/L) in the presence or absence of sulfide donors NaSH, GYY4137, AP67, & AP72 (200 μmol/L) at 37°C for 90 minutes. (c) Confluence HAoECs were exposed to the obtained Hb samples for 8 hours & VCAM-1 expression was determined by Western blotting. Representative experiment, n = 3. (d, lower panel) Confluence HAoECs cultured in ECIS plates were exposed to the obtained Hb samples & transendothelial electrical resistance was monitored by ECIS instrument for 3 hours. Representative experiment, n = 3, each performed in triplicate (d, upper panel). HAoECs grown on coverslips, upon reaching confluence cells were exposed to the Hb samples for 8 hours. Cells were stained for F-actin (phalloidin-TRITC, red) & DNA (Hoechst, blue). White arrows show intercellular gaps. Representative image, n = 5. ∗∗ indicates statistical significance (p < 0.001). ∗∗∗ indicates statistical significance (p < 0.0001). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29560080), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Western Blot: GAPDH Antibody (1D4) [NB300-221] - Upregulation & accumulation of the endogenous mouse GFAP in the GFAPTg mice.Urea-soluble fractions prepared from whole brains of GFAP+/+ wild type (A, lanes 1–3) & GFAPTg (A, lanes 4–6) mice were analyzed by immunoblotting using the anti-mouse GFAP antibody. Immunoblots probed with anti-GAPDH antibody was used as a loading control. Note that the endogenous mouse GFAP was significantly increased in the GFAPTg mice (A, lanes 4–6) compared to wild type controls (A, lanes 1–3). Approximate molecular weight markers (in kDa) were shown on the left. The distributions of human GFAP in relation to the endogenous mouse GFAP in brain sections of wild type (GFAP+/+, B) & GFAPTg (C-H) mice were visualized by double-label immunofluorescence microscopy using anti-mouse GFAP & SMI-21 antibodies. The immunofluorescence for human GFAP was in the green channel (C & F), whereas the counterstaining for mouse GFAP was in the red channel (D & G). Merged images showed the superimposition of both the green & red signals, with overlapping area appearing yellow (B, E, & H). Nuclei were revealed by staining with DAPI (B, E, & H). In wild type mice, normal appearance of GFAP in astrocytes was readily stained with the anti-mouse GFAP antibody (B), with very little staining with the SMI-21 antibody. Conversely, GFAPTg mice showed numerous Rosenthal fiber-like GFAP aggregates in the granular cell layer of the cerebellum (C-E) & the pial surface of the cortex (F-H), which were immunopositive for both mouse & human GFAP. Bar, 10 μm. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0180694), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: GAPDH Antibody (1D4) [NB300-221] - IL-6 negatively regulates EC differentiation: the effect of IL-6 on VEGF-A-stimulated differentiation of MSCs into ECs was examined. IL-6R & VEGFR-2 mRNA expression was analyzed by RT-PCR & normalized to GAPDH (n = 3) (a). Sox18 protein levels were measured by Western blot analysis & normalized to GAPDH (n = 3) (b). Expression of EC markers was determined by FACS analysis, & a representative grid is shown (n = 3–6) ((c)–(g)). Endothelial tube formation was examined using an angiogenesis assay (n = 3) ((d)–(h)). Experiments were performed with samples taken from independent BM-MSC cultures from separate microswine. HUVECs were excluded from statistical analyses. Data are shown as mean ± SD. ∗p < 0.05 versus naïve MSCs & #p < 0.05 MSCs treated with VEGF-A versus VEGF-A plus IL-6 cotreatment. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26106428), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Western Blot: GAPDH Antibody (1D4) [NB300-221] - Demonstration of the advantages of crude fractionation over whole cell lysis & scale up of the approach. (A) HEK293 cells were plated at a density of 4 × 105 cells per well of a 12 well plate & subsequently lysed directly in NP40 or RIPA lysis buffer or processed according to the protocol in Figure 2 (Sequential). An aliquot of each extract was then analyzed by 4-12% SDS PAGE followed by staining with Coomassie blue or by Western blotting & probing with antibodies to various marker proteins of specific intracellular organelles as previously. (B) HEK293 cells were plated at a density of 4 × 105 cells per well of a 12 well dish & then transfected the next day in triplicate with 400 ng of a construct encoding V5/6×-HIS tagged ERGIC-53. Cells were extracted 48 hours later either directly in RIPA buffer, directly in NP40 buffer or according to our extraction protocol. Proteins were then partially purified from each extract using Nickel resin (SIGMA #P6611) & eluted proteins were analyzed by 10% SDS PAGE followed by staining with Coomassie blue or by Western blotting & probing with the anti V5 antibody. (C) HEK293 cells were plated at a density of 4 × 105 cells per well of a 12 well dish & then transfected the next day in with 1600 ng of pcDNA6/V5-His (Invitrogen) or constructs encoding WT or MUT COMP. Cells were harvested 48 hours later & extracted according to our protocol. (D) HEK293 cells were plated at a density of 4 × 105 cells per well of a 12 well dish or 8.4 × 105 cells per well of a 35 mm dish & processed according to the protocol in Figure 2. An aliquot of each extract was then analyzed by 4-12% SDS PAGE followed by Western blotting & probing with antibodies to GAPDH, BiP & Lamin A. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/20003239), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: GAPDH Antibody (1D4) [NB300-221] - Co-culture of macrophages & prostate cancer cells increases prostate cancer cell migration & invasion & induces CCL2 secretionA. U937 differentiation to M2 macrophages is determined using western blot analysis. CCR7 (an M1-type macrophage marker) & CD206 (an M2-type macrophage marker) are assayed using proteins extracted from U937 cells treated with PMA for 24 h & exposed to CM of prostate cancer cells. B. Prostate cancer cells are placed in transwell inserts, & CM of U937 & U937-M cells is added. C. Prostate cancer cells are placed in transwell inserts with Matrigel®-coated membranes in the upper compartment, & U937-M cells are placed in the lower compartments. After 24-h incubation, the cells that had migrated through the membrane are stained. The mean optical density (OD) value is read using a microreader at 595 nm. Data are presented as mean ± SD. D. Chemokine arrays comparing the CM of PC-3 cells in monoculture & the CM of PC-3 cells co-cultured with monocyte cells. E. Prostate cancer cells are co-cultured with U937 cells for 24 h, CM is collected, & CCL2 levels are analyzed using ELISA. Adjustments of brightness, contrast, & size are applied to the whole images of western blot-based analyses without elimination of any information present in the original, including backgrounds. The mean OD value is read using a microreader at 450 nm, & data are presented as mean ± SD. All experiments are performed in triplicate, & the mean values are shown. *p < 0.05, **p < 0.01, ***p < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28039457), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - HMGB1-induced EMT in human airway epithelial cells.Human primary airway epithelial cells & BEAS-2B cells were treated with different doses of HMGB1 for mRNA analysis at different time points, & at 24 h for protein analysis. E-cadherin, ZO-1, & vimentin mRNA expression was detected by real-time quantitative PCR in (a) human primary airway epithelial cells & (c) in BEAS-2B cells after HMGB1 treatment (300 ng/mL) for 24 h. E-cadherin, ZO-1, & vimentin protein expression in (b) human primary airway epithelial cells andBEAS-2B cells (d) was assessed by western blot analysis. Data are expressed as mean ± SD (n = 3–5). *p < 0.05, **p < 0.01, ***p < 0.001, as compared with the control group. (e) TGF-beta 1 expression in cell lysate (LAP) was assessed by western blot analysis & in cell medium (active form) by ELISA. Quantification of protein expression was performed using ImageJ software. Data are expressed as mean ± S.D. (n = 4). In immunoblotting assay, gels have been run under the same experimental conditions. Then cropped blots were incubated with different primary antibodies for analysis of EMT markers expression. Original blots of (b) are presented in Supplementary Fig. 3. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26739898), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - Expression of CSE in human aortic valves. (a) Western blot of CSE protein from AS valve (N = 12) lysates & AI valve (N = 9) lysates (left panel) were performed. Representative CSE protein levels of three AS & three AI valves lysates were shown. Relative CSE levels were assessed by densitometry analyses of band intensities of CSE western blots normalized to GAPDH (panel right). (b) Zn2+ precipitated sulfide content under alkaline conditions was measured in AI (N = 18) & AS (N = 18) valve tissues normalized to protein content of the individual samples. (c) VIC derived from different AI (N = 6) & AS (N = 9) patients were cultured in calcification medium. CSE expression was measured after the initiation of calcification. Results were normalized to GAPDH of the samples. (d) Double immunohistochemistry of CSE‐SMA & CSE‐ALP was shown with two different magnifications (×400 magnification & ×1,000 magnification). Data shown are means ± SEM of N experiments. *P < .05, significantly different as indicated Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31017307), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Western Blot: GAPDH Antibody (1D4) [NB300-221] - Demonstration of the advantages of crude fractionation over whole cell lysis & scale up of the approach. (A) HEK293 cells were plated at a density of 4 × 105 cells per well of a 12 well plate & subsequently lysed directly in NP40 or RIPA lysis buffer or processed according to the protocol in Figure 2 (Sequential). An aliquot of each extract was then analyzed by 4-12% SDS PAGE followed by staining with Coomassie blue or by Western blotting & probing with antibodies to various marker proteins of specific intracellular organelles as previously. (B) HEK293 cells were plated at a density of 4 × 105 cells per well of a 12 well dish & then transfected the next day in triplicate with 400 ng of a construct encoding V5/6×-HIS tagged ERGIC-53. Cells were extracted 48 hours later either directly in RIPA buffer, directly in NP40 buffer or according to our extraction protocol. Proteins were then partially purified from each extract using Nickel resin (SIGMA #P6611) & eluted proteins were analyzed by 10% SDS PAGE followed by staining with Coomassie blue or by Western blotting & probing with the anti V5 antibody. (C) HEK293 cells were plated at a density of 4 × 105 cells per well of a 12 well dish & then transfected the next day in with 1600 ng of pcDNA6/V5-His (Invitrogen) or constructs encoding WT or MUT COMP. Cells were harvested 48 hours later & extracted according to our protocol. (D) HEK293 cells were plated at a density of 4 × 105 cells per well of a 12 well dish or 8.4 × 105 cells per well of a 35 mm dish & processed according to the protocol in Figure 2. An aliquot of each extract was then analyzed by 4-12% SDS PAGE followed by Western blotting & probing with antibodies to GAPDH, BiP & Lamin A. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/20003239), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

$Western Blot: GAPDH Antibody (1D4) [NB300-221] - Effect of forskolin on the surface expression of CFTR. (A) Quantitation & representative blot of cell surface biotinylation of CFTR in HEK‐CFTR cells that were treated with forskolin (FSK; 10 μmol/L) for 1, 4, & 10 min. GAPDH was used as a control to determine if there was any contamination of biotinylated protein in the nonbiotinylated fractions (Ab: monoclonal mouse‐anti‐CFTR‐C & anti‐GAPDH; 1:1000 & 1:2000 dilution, respectively; estimated sizes: for CFTR: 165 kDa & GAPDH: 36 kDa). (B) Effect of FSK on CFTR location in live HEK‐CFTR cells. Cells grown in 35‐mm glass‐bottom dishes were stained as described in the Methods. Images were captured before & after the treatment of FSK as time series. Snapshots at 0, 1, 4, & 10 min are shown. Green: CFTR; red: WGA; & blue: Dapi. White arrows: colocalization of CFTR & WGA; green arrows: CFTR vesicles. n ≥3 for all experiments. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25263207), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: GAPDH Antibody (1D4) [NB300-221] - HER2/HER3 & AXL expression & phosphorylation analysis.A) Representative western blots of total cell lysates of HCC827 & HCC4006 parental cell lines (P) & their derived ERL-resistant cell lines. Arrows indicate the expected molecular weight size. Total cell lysates loaded were 40 μg for AXL & pAXL analyses & 25 μg for the others. B) qPCR analysis of AXL mRNA normalized to rp-L31 mRNA & expressed relative to the levels in parental cell lines set as 1 (mean ± SD of triplicate determinations). Western blots & qPCR data are representative of those obtained respectively from 3 & 2 independent analysis. C) Dose-effect curves were calculated using CompuSyn software & plotting the entered Fa values against the entered dose values. For combination treatments, the combined drugs dose was entered. Each data point represents the mean of 3 replicates. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0143333), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - Ang II positively regulates VEGF-A-mediated EC differentiation: the effect of Ang II on VEGF-A-stimulated differentiation of MSCs into ECs was examined. AT2R & VEGFR-2 mRNA expression was analyzed by RT-PCR (n = 3) (a). Sox18 protein levels were measured by Western blot analysis (n = 3) (b). Expression of EC markers was determined by FACS analysis, & a representative grid is shown (n = 5-6) ((c)–(g)). Endothelial tube formation was examined using an angiogenesis assay (n = 3) ((d)–(h)). Experiments were performed with samples taken from independent BM-MSC cultures from separate microswine. HUVECs were excluded from statistical analyses. Data are shown as mean ± SD. ∗p < 0.05 versus naïve MSCs & #p < 0.05 MSCs treated with VEGF-A versus VEGF-A plus Ang II cotreatment. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26106428), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Western Blot: GAPDH Antibody (1D4) [NB300-221] - Expression of Npr2 & cGKI alpha in DRGs at different developmental stages. (A,B) Western blot of membrane or cytosolic fractions of DRGs using antibodies to Npr2 or to cGKI alpha , respectively. The heavy chain of clathrin or GAPDH served as loading control. (C–E) Sections through thoracic DRGs at different stages. Localization of anti-beta Gal staining indicating Npr2-expression is demonstrated in the Npr2wt/LacZ-mouse reporter & localization of cGKI alpha by a polyclonal antibody to mouse cGKI alpha . Scale bars in (C1,D1), 50 μm; in (C2-C5,D2-D5), 100 μm; in (E) 25 μm. (F) Quantification of Npr2-positive & cGKI alpha -positive neurons in DRGs counterstained with an antibody to PGP9.5 at different stages. (G–I) A small proportion of Npr2-positive DRG neurons at P45 & P75 express trkA, parvalbumin, CGRP or IB4. Scale bars in (H,I), 20 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29472841), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: GAPDH Antibody (1D4) [NB300-221] - Bub1-KD & Bub1-T589A display increased residency in the cytosol.(a) Mitotic control (siGL2) & Bub3-depleted (siBub3) cells were fixed & stained with anti-H2A-pT120 (red), anti-Sgo1 (green) & anti-CREST (blue). (b) Quantification of the localization of H2A-pT120 & Sgo1 signals. Data represent the mean±s.e. of three independent experiments. Eighty to 300 cells were scored per condition per experiment. (c) Images & (d) quantification (normalized average pixel intensity); low (1–1.2), medium (>1.2 to ≤1.3) & high (>1.3) of 3 × MYC-GFP-Bub1 signal & localization in live cells synchronized in mitosis by a thymidine release. Data represent the mean±s.e. of 3 independent experiments, with 58–61 cells measured per condition. Significance was measured for the high group by one-way analysis of variance (ANOVA) & pairwise t-test (Holm–Sidak). (e) Scatter plot of the cytoplasm versus kinetochore GFP levels of individual cells from each of the stable cell lines. The number of cells, R2 (measure of the goodness-of-fit) & significance (one-way ANOVA) are indicated. (f) Western blottings showing levels of the 3 × MYC-GFP-Bub1 proteins in the stable cell lines in whole cell extracts (left) & in cytoplasmic extracts (right). Scale bar, 10 μM. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/ncomms9364), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Western Blot: GAPDH Antibody (1D4) [NB300-221] - Notch1, ApoER2 & Dab1 colocalize in hippocampal neurons. (A) Representative image of fluorescent immunolabeling shows that Notch1 is localized in a subset of CA3 neurons, co-expressing Dab1 & ApoER2 (magnified insert). ApoER2 is highly expressed in all CA3 neurons. (B) Fluorescent immunolabeling shows the distribution of Notch1 & Dab1 as compared to Arc/Arg3.1 in CA3 neurons. (B′) Close up of a dendrite showing colocalization of the three proteins (white arrowheads). (C) Western blot analysis on immunoprecipitated samples from whole hippocampal lysate shows that Notch1 displays a strong interaction with Dab1 whereas Notch1 & ApoER2 interaction appears weaker in the preparation (n = 4 independent experiments). (D) Immunolabeling on immunoprecipitated samples from whole cortical lysates show that Notch1 & Dab1 interact. ApoER2 is bound to both Notch1 & Dab1 (n = 3 independent experiments). (E) Co-IP from synaptosomal membrane fractions reveals a stronger interaction between Notch1 & ApoER2, which is reduced in the N1cKO (n = 3 independent pulldowns). In (C–E) GAPDH is used as a loading control for the inputs & to detect contamination in the IP samples. Scale bar in (A) is 50 μm & (B) 25 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26635527), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

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.

$Western Blot: GAPDH Antibody (1D4) [NB300-221] - Role of the TRIM11-USP14 axis in cell growth & apoptosis. a Levels of endogenous TRIM11 in HCT116 cells grown at 43 °C for 0 or 90 min, or at 43 °C for 90 min, & then at 37 °C for 60 or 120 min. b, c Levels of endogenous TRIM11 (b), or Flag-TRIM11, the indicated proteasome subunits, & USP14 (c) in the SN & P fractions of HCT116 cells with & without heat shock at 43 °C for 90 min. d, g TRIM11 overexpression (d) or knockdown (g) HCT116 cells & the corresponding control cells grown under unstressed, heat shock, & heat shock plus recovery conditions were analyzed for K48 polyUb conjugates & caspase-3 activation. e, f, h Apoptosis in TRIM11 overexpression (e, f) or knockdown (h) HCT116 cells, & the corresponding control HCT116 cells, treated with & without heat shock. i, j Caspase-3 activation (i) & apoptosis (j) in HCT116 cells expressing the indicated proteins and grown under normal or heat stress conditions. k–m K48 polyUb conjugates, caspase-3 activation (k), amyloid-like fibrils (l), & apoptosis (m) in HCT116 cells expressing the indicated proteins and grown under normal & heat stress conditions. In e, f, h, j, l, & m, data represent mean ± SEM (n = 3 unless otherwise indicated). *P < 0.05; **P < 0.01; ***P < 0.001. Uncropped blots are presented in Supplementary Fig. 14 Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-018-03499-z), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Reactivity:

Hu, Mu, Rt, Po, Av, Bv, Ca, Ch, ChHa, Dr, Eq, Fe, Ha, Ma-Op, Pm, Rb, Sh, Ze

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Av, Bv, Ca, Ch, ChHa, Dr, Eq, Fe, Ha, Ma-Op, Pm, Rb, Sh, Ze

Applications:

, , , , , , ,

Applications: , , , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Validated by:

Validated by:

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB300-221SS

compare

(select up to 3 products from this page to compare)

NB100-56875

GAPDH Antibody - BSA Free

(5 Reviews)

(131 Publications)

0.1 mg

NB100-56875

$Western Blot: GAPDH Antibody [NB100-56875] - Analysis of GAPDH using this antibody at 1:500 in nuclear and cytoplasmic fractions made from Drosophila head extracts. Data courtesy of Dr. Jerry Lin, University of Wisconsin-Madison.$

Western Blot: GAPDH Antibody [NB100-56875] - Analysis using HeLa cells. Theoretical molecular weight: 36 kDa.

<b>Biological Strategies Validation. </b>GAPDH-Antibody-Western-Blot-NB100-56875-img0010.jpg

Simple Western: GAPDH Antibody [NB100-56875] - Lane view shows a specific band for GAPDH in 0.5 mg/ml of HeLa lysate. This experiment was performed under reducing A246conditions using the 12-230 kDa separation system. Note: band observed higher than predicted 36 kDa molecular weight.

$Western Blot: GAPDH Antibody [NB100-56875] - Vps13 co-fractionates with Rab7 & Rab5.(A) Western blot analysis of control fly head samples fractionated into a cytosolic & membrane fraction from postnuclear supernatant (PNS). EGFR was used as a membrane marker & GAPDH as a cytosolic marker. (B) Membrane fractions from control fly heads treated with 1 M KCl, Na2CO3 pH 11 or 6 M urea were centrifuged to separate the soluble & insoluble (membrane containing) fractions. The level of Vps13 was determined in these fractions. Markers for peripheral membrane proteins (GM130), integral membrane proteins (EGFR) & the cytosolic proteins (GAPDH) were used. The “Vps13 lysate” lane contains a lysate derived from Vps13 homozygous mutant fly heads, as expected no Vps13 is detected, demonstrating the specificity of the antibody against Vps13. (C) Membranes from control fly heads were fractionated on a sucrose gradient. Western blot analysis was performed to analyze the distribution of Vps13 in relation to markers associated with membranes of various organelles: Rab7 (late endosomes), Rab5 (early endosomes), GM130 (golgi), Lamp1 (lysosomes) & ATP5A (mitochondria). (D) Immunoisolation of membranes from fraction 14 of the sucrose gradient using Vps13 NT, Rab7 & Rab5 antibodies. (E) Quantification of the sucrose gradient fractionation of Fig 2C. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28107480), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

$Western Blot: GAPDH Antibody [NB100-56875] - Overexpression of HsVps13A rescues phenotypes of Vps13 mutants.(A) Samples from fly heads of Actin-GAL4 / + (as a control) & Actin-GAL4 / UAS-HsVps13A (HsVps13A expressing) flies were separated into a membrane & cytosol fraction & analyzed by Western blot for HsVps13A levels. EGFR & GAPDH used as controls for membrane & cytosolic proteins, respectively. (B) Eclosion rate of Vps13 mutant flies a Actin-GAL4/+ (control) or Actin-GAL4/UAS-HsVp13A (HsVps13A expressing) background at 25°C. (C) Ubiquitylated proteins from samples of 1 day old fly head extracts of Vps13/CyO; Actin-GAL4/+ (as a control), Vps13/ Vps13; Actin-GAL4/+ (representing homozygous mutants) & Vps13/ Vps13; Actin-GAL4/UAS-HsVps13A (representing homozygous mutants expressing human VPS13A). (D) Representative picture of ubiquitylated protein staining of the third instar larval ventral nerve cord of Vps13/CyO; Actin-GAL4/+ (as a control), Vps13/ Vps13; Actin-GAL4/+ & Vps13/ Vps13; Actin-GAL4/UAS-HsVps13A. Arrows indicate accumulations of ubiquitylated positive structures. The scale bar indicates 50 μm & 12,5 μm in the enlargement. (E) Quantification of the number of puncta in third instar larval ventral nerve cord of the experiment presented in Fig 6D. (F) Life span curve of Vps13/ Vps13; Actin-GAL4/+ & Vps13/ Vps13; Actin-GAL4/UAS-HsVps13A. All quantifications show the mean & SEM of at least three independent experiments per condition. For statistical analysis a two-tailed students T-test was used in combination with a Welch’s correction if necessary. P<0.05 is *, P<0.01 is ** & P<0.001 is ***. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28107480), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: GAPDH Antibody [NB100-56875] - No dystrophin expression was detected in cardiac & skeletal muscles of Dmdmdx rats.(A) Male 7 month-old rats of line 61, wild-type littermate controls (WT) & Dmdmdx were sacrificed & biopsies from tibialis cranialis muscles (TC) & hearts (H) were harvested. Western-blot of total proteins (50 µg) was incubated with NCL-DYS2 & Manex1011C monoclonal antibodies (C-terminal & exons 10/11 epitopes, respectively). This revealed undetectable levels of the 427 kDa dystrophin band in line 61 Dmdmdx rats. Muscle from a GRMD dog (GD) was used as negative control & samples from WT rats were used as positive controls. Staining with an anti-GAPDH polyclonal antibody validated equal protein loadings. (B–E) Heart & biceps femoris muscles from the same wild-type (B & C) & Dmdmdx rats (D & E) were assessed for dystrophin expression using immunohistochemistry with Mandys110 monoclonal antibody (against exons 38–39 epitope). Compared to the subsarcolemmal expression of dystrophin in wild-type muscles, no dystrophin was detected in Dmdmdx rats except for the presence in skeletal muscle of only rare scattered revertant positive fibers (arrowheads). Immunolabelling of dystrophin (B–E) Bar = 100 µm. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0110371), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody [NB100-56875] - ABCA1, ABCG1 & SR-BI protein expressions. a & b Hepatic protein expressions of ABCA1, ABCG1 & SR-BI were significantly decreased in COMT−/− mice at GD 18.5, compared to C57BL/6 J mice. Decreased hepatic ABCA1 expression was also observed at 10 days postpartum. ATI-5261 increased ABCA1 & ABCG1 expression in the liver at 10 days postpartum. c Placental protein expressions of ABCA1 & ABCG1 was reduced in COMT−/− mice, compared to C57BL/6 J mice. ATI-5261 treatment significantly increased ABCA1 levels in the placenta of COMT−/− mice. d Representative immunoblots of the corresponding proteins in the placenta with mouse RAW264.7 cell lysate included as positive control. Similar results were obtained when the experiment was repeated with lysates prepared from three batches of tissues. Data are presented as mean ± SEM. Groups (n = 8 in all groups) were compared using one-way ANOVA with post-hoc analysis (Tukey’s procedure). *, p < 0.05 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30237900), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Western Blot: GAPDH Antibody [NB100-56875] - Vps13 co-fractionates with Rab7 & Rab5.(A) Western blot analysis of control fly head samples fractionated into a cytosolic & membrane fraction from postnuclear supernatant (PNS). EGFR was used as a membrane marker & GAPDH as a cytosolic marker. (B) Membrane fractions from control fly heads treated with 1 M KCl, Na2CO3 pH 11 or 6 M urea were centrifuged to separate the soluble & insoluble (membrane containing) fractions. The level of Vps13 was determined in these fractions. Markers for peripheral membrane proteins (GM130), integral membrane proteins (EGFR) & the cytosolic proteins (GAPDH) were used. The “Vps13 lysate” lane contains a lysate derived from Vps13 homozygous mutant fly heads, as expected no Vps13 is detected, demonstrating the specificity of the antibody against Vps13. (C) Membranes from control fly heads were fractionated on a sucrose gradient. Western blot analysis was performed to analyze the distribution of Vps13 in relation to markers associated with membranes of various organelles: Rab7 (late endosomes), Rab5 (early endosomes), GM130 (golgi), Lamp1 (lysosomes) & ATP5A (mitochondria). (D) Immunoisolation of membranes from fraction 14 of the sucrose gradient using Vps13 NT, Rab7 & Rab5 antibodies. (E) Quantification of the sucrose gradient fractionation of Fig 2C. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28107480), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Simple Western: GAPDH Antibody [NB100-56875] - Analysis of non-canonical inflammasome pathway.A LDH cytotoxicity assay in the presence of LPS or SCGB3A2 alone, or the two together (SCGB3A2 + LPS). B LDH cytotoxicity assay in the presence of various amount of nigericin. Average ± SD from more than three independent experiments. *P < 0.01, **P < 0.0001 by Tukey’s multiple comparison. C Morphology of cells cultured in the presence of LPS or SCGB3A2 alone, SCGB3A2 + LPS, or nigericin for 3 h. For nigericin-treated group, cells were primed with LPS before addition of nigericin. Black arrow indicates ballooned cells, characteristic feature of pyroptosis. D Western blotting for the cleaved forms of CASP1 (p20), CASP4 (p20), & GSDMD (N-terminal). S: SCGB3A2, N: nigericin. Experiments were repeated more than twice & same results were obtained. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33452234), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Ca, Dr, Fe, Ha, Pm, Ma

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Ca, Dr, Fe, Ha, Pm, Ma

Applications:

, , , ,

Applications: , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Alt Catalog#

IMG-5143A

Alt Catalog# IMG-5143A

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Validated by:

Validated by:

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-56875SS

compare

(select up to 3 products from this page to compare)

2275-PC-100

GAPDH Antibody [Unconjugated]

(112 Publications)

100 uL

2275-PC-100

HAF008). A specific band was detected for GAPDH at approximately 36 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." class="big_lightbox">

Western blot shows lysates of U2OS human osteosarcoma cell line, A20 mouse B cell lymphoma cell line, and L6 rat myoblast cell line. PVDF membrane was probed with 0.1 µg/mL Rabbit Anti-Human/Mouse/Rat GAPDH Polyclonal Antibody (Catalog # 2275-PC) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog # <a class=

HAF008). A specific band was detected for GAPDH at approximately 36 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." alt="Western blot shows lysates of U2OS human osteosarcoma cell line, A20 mouse B cell lymphoma cell line, and L6 rat myoblast cell line. PVDF membrane was probed with 0.1 µg/mL Rabbit Anti-Human/Mouse/Rat GAPDH Polyclonal Antibody (Catalog # 2275-PC) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog # HAF008). A specific band was detected for GAPDH at approximately 36 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." class="big_thumb" />

Simple Western shows lysates of Exosome Standards (LNCaP) (NBP3-11687), Exosome Standards (HT‑29) (NBP3-11685) and Jurkat human acute T cell leukemia cell line, loaded at 0.5 mg/ml. A specific band was detected for GAPDH at approximately 41 kDa (as indicated) using 5 µg/mL of Rabbit Anti-Human/Mouse/Rat GAPDH Antigen Affinity-purified Polyclonal Antibody (Catalog # 2275-PC-100). This experiment was conducted under reducing conditions and using the 12-230kDa separation system.

Simple Western lane view shows lysates of Jurkat human acute T cell leukemia cell line, C2C12 mouse myoblast cell line, and C6 rat glioma cell line, loaded at 0.2 mg/mL. A specific band was detected for GAPDH at approximately 43 kDa (as indicated) using 1 µg/mL of Rabbit Anti-Human/Mouse/Rat GAPDH Antigen Affinity-purified Polyclonal Antibody (Catalog # 2275-PC-100) . This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.

Higher levels of CD4 are found in macrophages expressing LCK.A) Schematic diagram of self-inactivating lentiviral construct used to express wild-type Lck and puroR (LCKWT P). A similar construct was used to express a kinase inactive form of Lck and puroR (LCKINACTIVE P) or to express puroR only (‘control P’). B) Detection of protein expression of LCK and CD4. Control and transgenic PSC-macrophages lysates were analysed by western blotting using anti-LCK and anti-CD4 antibodies. The loading control GAPDH was detected using anti-GAPDH antibody. C) Protein levels were measured with Odyssey software (Li-COR) and CD4 expression was normalised to GAPDH expression. Symbols represent normalised CD4 expression, relative to the PSC-macrophages control group, of two independent experiments. D) Detection of surface CD4 and total LCK expression. Representative two-colour immunofluorescence (dot plot) analysis is shown. Gates were determined by using the two relevant isotype control antibodies. Quantification of total LCK expression (E) and surface CD4 expression (F), expressed as the ratio of the geometric mean fluorescence intensity (MFI) over the isotype control ±SEM of independent experiments (n = 7). G) Detergent resistance of CD4, expressed as mean Flow Cytometric Detergent Resistance (FCDR) index of CD4 (n = 4) in PSC-macrophages, calculated as described in materials and methods. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24465876), licensed under a CC-BY license. Not internally tested by R&D Systems.

CD4 knock-down in genetically modified stem cell-derived macrophages. C) Detection of protein expression of CD4. Control and transgenic PSC-macrophages lysates were analysed by western blotting using anti-CD4 antibodies. GAPDH, a loading control, was detected using anti-GAPDH antibody. Representative blot is shown. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24465876), licensed under a CC-BY license. Not internally tested by R&D Systems.

Reactivity:

Hu, Mu, Rt

Species Glossary

Reactivity: Hu, Mu, Rt

Applications:

, ,

Applications: , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Conjugate:

Unconjugated

compare

(select up to 3 products from this page to compare)

NB600-502

GAPDH Antibody (6C5cc) - BSA Free

(3 Reviews)

(87 Publications)

0.2 mg

NB600-502

Western Blot: GAPDH Antibody (6C5) [NB600-502] - Western blot of FGF23 in the kidney. GAPDH antibody (6C5) served as an internal control. Each value represents the mean +/- SEM. Citation: Sugiura H, Matsushita A, Futaya M, Teraoka A, Akiyama K-i, Usui N, et al. (2018) Fibroblast growth factor 23 is upregulated in the kidney in a chronic kidney disease rat model. PLoS ONE 13(3): e0191706. //doi.org/10.1371/journal.pone.0191706

Simple Western: GAPDH Antibody (6C5) [NB600-502] - Simple Western lane view shows a specific band for GAPDH in 0.5 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system. Note: band observed higher than predicted 36 kDa molecular weight.

Simple Western: GAPDH Antibody (6C5) [NB600-502] - Anaylsis in rat brain and spinal cord. This image includes the GAPDH at the predicted kDa as well as a glucocorticoid receptor antibody (peak 102). Verified customer review.

Western Blot: GAPDH Antibody (6C5cc) [NB600-502] - Western blot analysis for whole cell & nuclear signal transduction proteins. (A) Phosphorylated FAK (Y397) was significantly decreased at 24 h & significantly increased at 48 h as compared to sham. (B) Nuclear localization of corresponding signal transduction molecules, p38, & p65, were decreased at 24 h & increased at 48 h as compared to sham. *p < 0.05, #p = 0.056, Data are represented as mean ± SEM, whole cell: n = 9–10/group; nuclear: n = 7–9/group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30853931), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (6C5cc) [NB600-502] - Upregulation of innate immune response genes in BRCA2-deficient human cells. a Venn diagram of common genes upregulated in H1299 & MDA-MB-231 human cells, upon chronic (28 days) DOX-induced BRCA2 depletion. b Gene set enrichment analysis (Gene Ontology—Biological Process database) of the 28 genes upregulated upon chronic BRCA2 inactivation in both H1299 & MDA-MB-231 cells. c, d Whole-cell extracts prepared after 4 & 28 days of DOX treatment were immunoblotted as indicated. GAPDH was used as a loading control. Phosphorylation site are indicated in red Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31316060), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (6C5cc) [NB600-502] - FGF23 expression in the partial nephrectomy rat model.(a) Serum FGF23 concentration. (b) FGF23 mRNA expression in the kidney. Sham group was used as a normalization control. (c) Western blot of FGF23 in the kidney. (d) Histology in the kidney. HE: hematoxylin-eosin staining. MT: Masson’s trichrome staining to evaluate fibrosis. VK: Von Kossa staining to evaluate calcification. *P<0.05, **P<0.01, ***P<0.001; sham group (n = 6), partial nephrectomy mild group (PN mild) (n = 6), partial nephrectomy severe group (PN severe) (n = 6). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29518087), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (6C5cc) [NB600-502] - FGF23 expression in hemi-nephrectomized rats fed a high-P diet.(a) Serum FGF23 concentration. (b) FGF23 mRNA expression in the bone. NP sham group was used as a normalization control. (c) FGF23 mRNA expression in the kidney. NP sham group was used as a normalization control. (d) Western blot of FGF23 in the kidney. GAPDH was used as an internal control. Each value shown represents the mean ± SEM; *P<0.05, **P<0.01; NP sham group (n = 8), NP Nx group (n = 7), HP sham group (n = 7) & HP Nx group (n = 9). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29518087), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (6C5cc) [NB600-502] - Time course of innate immune response activation in BRCA2-deficient cells. a H1299 cells expressing a DOX-inducible BRCA2 shRNA were grown in the presence or absence of DOX for 28 days. Cells collected every 2 days were subjected to quantitative RT-PCR analyses using primers specific for indicated genes. mRNA levels were expressed relative to the gene encoding beta -actin & to day 2 (2− delta delta CT). n = 3 independent experiments, each performed in triplicates. Each dot represents a single replicate. b Whole-cell extracts prepared at indicated times after DOX addition were immunoblotted as shown. GAPDH was used as a loading control. Phosphorylation sites are indicated in red Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31316060), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (6C5cc) [NB600-502] - Decreased proliferation rates in ALDH2‐deficient human fibroblasts upon HR abrogationA–CHuman fibroblasts carrying either WT ALDH2 or the E487K homozygous ALDH2 mutation were transfected with control (SCR) or siRNAs against BRCA1 (A), BRCA2 (B), or RAD51 (C). Cells were processed for proliferation assays 48 h after transfection. siRNAs were retransfected at an interval of 4 days. Graphs are representative of three independent experiments, each performed with three technical replicas. Error bars represent SD of three technical replica values obtained from a single experiment. Cell extracts were prepared 48 h after transfection & immunoblotted as shown. SMC1 or GAPDH were used as loading controls. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28729482), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (6C5cc) [NB600-502] - CtIP is not required for degradation of the single-stranded telomeric overhang generated by TRF2 inactivationImmortalized MEFs were infected with retroviruses expressing the indicated shRNAs, followed by selection with puromycin for 72 h. Cell extracts were prepared 48 h later & analysed by Western blotting as indicated. SMC1 & GAPDH were used as loading controls. *non-specific band.MboI- & AluI-digested DNA from cells treated as in (A) was resolved by pulsed-field gel electrophoresis & probed with end-labelled (AACCCT)4 probe. Representative pulsed-field gel samples run under native & denatured conditions are shown.Quantification of the 3′ overhang in cells treated as in (B). For each sample, the ss/total DNA ratios were expressed relative to the GFP shRNA-treated control. Error bars represent SD of two independent experiments. 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.

Western Blot: GAPDH Antibody (6C5cc) [NB600-502] - ISG induction in HR-deficient human cells & tumors & olaparib impact on this process. a Upregulation of innate immune response genes in BRCA2-deleted ovarian tumors (n = 4) versus tumors with median BRCA2 mRNA expression (n = 145). b Upregulation of innate immune response genes in RAD51-deleted ovarian tumors (n = 11) versus tumors with median RAD51 mRNA expression (n = 145). Dots in graphs represent individual tumors. Middle line (white), median; box limits 25 & 75 percentiles; whiskers, minimum & maximum values. c H1299 cells expressing a DOX-inducible BRCA2 shRNA were grown in the presence or absence of DOX for 4 days. Then, olaparib (1 or 10 µM) was added for 72 h, followed by quantitative RT-PCR analyses. Primers specific for the indicated genes were used. mRNA levels were expressed relative to the gene encoding beta -actin & to untreated (−DOX) control cells (2− delta delta CT). Error bars represent SD of n = 3 independent experiments. *, p < 0.05 (unpaired two-tailed t test). d Whole-cell extracts from cells treated as in (c) were immunoblotted as shown. GAPDH & SMC1 were used as loading controls. Phosphorylation sites are indicated in red. e Cells treated as in (c) were pulse-labeled with EdU for 30 min. Frequency of cells in G1, S, & G2/M stages of the cell cycle were determined using FACS analyses of EdU incorporation & propidium iodide staining. Error bars represent SD of n = 3 independent experiments Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31316060), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (6C5cc) [NB600-502] - BRCA1 & CtIP mediate Ku- & LIG4-independent telomere fusionsImmortalized Brca1F/− MEFs were infected with retroviruses expressing the indicated shRNAs and/or Cre recombinase, followed by selection with puromycin for 72 h. Mitotic chromosomes isolated 48 h later were fixed & stained with a Cy3-conjugated (CCCTAA)3-PNA probe. The frequency of end-to-end chromosome-type fusions is represented as a percentage of fusions observed after TRF2 depletion. A minimum of 2,000 chromosomes were scored for each sample. Error bars represent SD of three independent experiments. P-values were calculated using an unpaired two-tailed t-test. NS, P > 0.05.Immortalized Brca1F/C61G MEFs were infected with retroviruses expressing the indicated shRNAs and/or Cre recombinase, followed by selection with puromycin for 72 h. The frequency of end-to-end chromosome-type fusions was analysed as in (A).MEFs of the indicated genotypes were infected with retroviruses expressing TRF2 and/or CtIP shRNAs, followed by selection with puromycin for 72 h. Cell extracts were prepared 48 h later & analysed by Western blotting as indicated. GAPDH was used as a loading control. *non-specific band. Cells treated as in (C) & (E) were arrested in mitosis with colcemid, & mitotic chromosomes isolated 48 h later were fixed & stained with a Cy3-conjugated (CCCTAA)3-PNA probe (D, F). The frequency of end-to-end chromosome-type fusions is represented as a percentage of fusions observed after TRF2 depletion. Error bars represent SD of two independent experiments. P-values were calculated using an unpaired two-tailed t-test. *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.

Reactivity:

Hu, Mu, Rt, Po, Am, Ca, ChHa, Fe, Fi, Rb, Bv(-), Gt(-)

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Am, Ca, ChHa, Fe, Fi, Rb, Bv(-), Gt(-)

Applications:

, , , , ,

Applications: , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB600-502AF350-0.2ml
Alexa Fluor 405	NB600-502AF405-0.2ml
Alexa Fluor 488	NB600-502AF488-0.2ml
Alexa Fluor 532	NB600-502AF532-0.2ml
Alexa Fluor 594	NB600-502AF594-0.2ml
Alexa Fluor 647	NB600-502AF647-0.2ml
Alexa Fluor 700	NB600-502AF700-0.2ml
Alexa Fluor 750	NB600-502AF750-0.2ml
Biotin	NB600-502B-0.2ml
CoraFluor 1	NB600-502CL1
DyLight 350	NB600-502UV-0.2ml
DyLight 405	NB600-502V-0.2ml
DyLight 488	NB600-502G-0.2ml
DyLight 550	NB600-502R-0.2ml
DyLight 594	NB600-502DL594-0.2ml
DyLight 650	NB600-502C-0.2ml
DyLight 680	NB600-502FR-0.2ml
DyLight 755	NB600-502IR-0.2ml
FITC	NB600-502F-0.2ml
HRP	NB600-502H-0.2ml
Janelia Fluor 525	NB600-502JF525
Janelia Fluor 549	NB600-502JF549-0.2ml
Janelia Fluor 646	NB600-502JF646-0.2ml
Janelia Fluor 669	NB600-502JF669
mFluor Violet 450 SE	NB600-502MFV450
mFluor Violet 500 SE	NB600-502MFV500
mFluor Violet 610 SE	NB600-502MFV610

compare

(select up to 3 products from this page to compare)

NB300-320

GAPDH Antibody

(2 Reviews)

(69 Publications)

0.1 mg

NB300-320

Immunohistochemistry-Paraffin: GAPDH Antibody [NB300-320] - Staining of paraffin embedded Human Pancreas. Antibody at 2.5 ug/mL. Steamed antigen retrieval with citrate buffer pH 6, AP-staining.

Western Blot: GAPDH Antibody [NB300-320] - Staining of HEK293 (A) and HeLa (B) cell lysate (35 ug protein in RIPA buffer). Antibody at 0.001 ug/mL. Detected by chemiluminescence. Approx 36 kDa band observed in lysates of cell line HEK293 and approx. 35 kDa in HeLa cell lysates.(calculated MW of 36.1 kDa according to Human NP_002037.2).

Immunocytochemistry/Immunofluorescence: GAPDH Antibody [NB300-320] - Immunofluorescence analysis of paraformaldehyde fixed A549 cells, permeabilized with 0.15% Triton. Primary incubation 1hr (10 ug/mL) followed by Alexa Fluor 488 secondary antibody (2 ug/mL), showing cytoplasmic and vesicle staining. The nuclear stain is DAPI (blue). Negative control: Unimmunized goat IgG (10 ug/mL) followed by Alexa Fluor 488 secondary antibody (2 ug/mL). Strong expression of the protein seen in the cytoplasm and vesicles of A549 cells.

GAPDH-Antibody-Immunohistochemistry-Paraffin-NB300-320-img0006.jpg

Upregulation of GAPDH & Tom20 in C6 gliomas. a A section of rat brain stained with hematoxilin & eosin to show a glioma produced by implantation of C6 cells in the right caudate nucleus. In this case, cells also grew in the region of the syringe needle track through the cortex. (b–d). A small glioma labeled by bisbenzamide (b) & with antibodies against Tom20 (c) & GAPDH (d). The brightness & contrast have been increased. e Illustration of a strip perpendicular to the rim of a glioma (labeled with bisbenzamide) & along which intensity profiles were measured. f, g Tom20 & GAPDH fluorescence along such a strip (barely visible without enhancement). The graphs show the raw intensity values given by ImageJ. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26032618), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody [NB300-320] - PAR2 causes contraction of smooth muscle cells from human prostate. (A & B) Decrease in diameter of collagen hydrogels after PAR2 activation with SLIGKV (80 µM). (C) Representative western blot & (D) densitometry showing time dependent increase in level of phosphorylated MLC20 in PSMC after PAR2 is activated. Data represent mean ± SEM of at least three independent experiments. Diameter of collagen hydrogels were measured in ImageJ (version 1.50i) & significance analyzed in Prism (version 7.04) with one‐way ANOVA followed by Tukey's multiple comparison test. *P < 0.05, **P < 0.01 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31198907), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: GAPDH Antibody [NB300-320] - Upregulation of GAPDH & Tom20 in C6 gliomas. a A section of rat brain stained with hematoxilin & eosin to show a glioma produced by implantation of C6 cells in the right caudate nucleus. In this case, cells also grew in the region of the syringe needle track through the cortex. (b–d). A small glioma labeled by bisbenzamide (b) & with antibodies against Tom20 (c) & GAPDH (d). The brightness & contrast have been increased. e Illustration of a strip perpendicular to the rim of a glioma (labeled with bisbenzamide) & along which intensity profiles were measured. f, g Tom20 & GAPDH fluorescence along such a strip (barely visible without enhancement). The graphs show the raw intensity values given by ImageJ. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26032618), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody [NB300-320] - CDC20B was the protein effector regulated by hsa-miR-633. (a) CDC20B level was up-regulated after ox-LDL treatment revealed by Western blotting. (b) CDC20B level was decreased after the treatment of hsa-miR-633 mimics revealed by Western blotting. (c) CDC20B level was increased after the treatment of hsa-miR-633 inhibitor revealed by Western blotting. (d) The luciferase reporter plasmids were constructed as illustrated. (e) Relative luciferase activities after co-transfection CDC20B WT & hsa-miR-633/Control, or CDC20B Mut & hsa-miR-633/Control were measured. (f) The expression levels of two proliferation markers, Ki67 & PCNA after the treatment of si-CDC20B were measured using Western blotting. (g) Colony formation assay was conducted to examine the proliferation abilityafter the treatment of si-CDC20B. (h) Transwell migration & invasion assays were conducted to examine the migration & invasion abilities of VSMCs after the treatment of si-CDC20B. (i) Quantification results of (g). (j) Quantification results of (h). *P < 0.05, **P < 0.01, ***P < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35212610), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Simple Western: GAPDH Antibody [NB300-320] - MiR-34a affects stroke outcomes via interacting with cytochrome c. (A) WES system image showing CYC, VDAC & GAPDH expression from hemispheres of WT & miR-34a−/− mice at 6 h post-stroke. (B) Relative CYC expression normalized to GAPDH from the data generated by the WES system. CYC level is significantly decreased in ischemic hemispheres of WT mice but no significant changes in miR-34a−/− mice between contralateral hemispheres (Control) & ischemic hemispheres (Ischemia). N = 5 per group, **p < 0.01, One-way ANOVA followed by post hoc Tuckey’s test was used for data analysis. Data are expressed as mean ± S.D. (C) Relative VDAC expression normalized to GAPDH from the data generated by the WES system. VDAC was not significantly altered in WT mice nor miR-34a−/− mice. (D) Multiplexed WES system image showing CYC & GAPDH expression from purified pCECs of WT & miR-34a−/− mice (n = 10 per group, pooled cell samples) at 6 h post-stroke. (E) Relative CYC expression by normalization to GAPDH. A 2.8 fold decrease of CYC level was observed in WT mice but no changes were observed in miR-34a−/− mice between contralateral hemispheres & ischemic hemispheres. (F) A CYC reporter was coexpressed with a miR-34a plasmid, a miR-34a mimic, a miR-34c mimic, or a plasmid control in cultured cerebral vascular endothelial cells for 24 hours. Relative firefly luciferase activity was evaluated & normalized to renilla luciferase activity. Relative firefly luciferase activity was reduced by miR-34a plasmid & miR-34a mimic. The experiment was repeated 3 times & triplicates were used for each analysis. Data represents the mean ± S.D. *p < 0.05. One-way ANOVA followed by post-hoc Tuckey’s test was used for analysis. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32094435), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody [NB300-320] - Hsa-miR-633 inhibitor could reverse the si-circ_0008896 phenotypes. (a) CCK8 assay was conducted to measure cell viability after up-regulation of hsa-miR-633. (b) The expression levels of two proliferation markers, Ki67 & PCNA after up-regulation of hsa-miR-633 were measured using Western blotting. (c) CCK8 assay was conducted to measure cell viability after the treatment of si-circ0008896, hsa-miR-633 inhibitor & si-circ0008896+ hsa-miR-633 inhibitor. (d) The expression levels of two proliferation markers, Ki67 & PCNA after the treatment of si-circ0008896, hsa-miR-633 inhibitor & si-circ0008896+ hsa-miR-633 inhibitor were measured using Western blotting. (e) Colony formation assay was conducted to examine proliferation ability number of colonies after the treatment of si-circ0008896, hsa-miR-633 inhibitor & si-circ0008896+ hsa-miR-633 inhibitor. (f) Quantification results of (e). (g) Transwell migration & invasion assays were conducted to examine the migration & invasion abilities of VSMCs after the treatment of si-circ0008896, hsa-miR-633 inhibitor & si-circ0008896+ hsa-miR-633 inhibitor. (h) Quantification results of (g). *P < 0.05, **P < 0.01, ***P < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35212610), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody [NB300-320] - Down-regulation of hsa_circ_0008896 inhibited proliferation, migration & invasion in vitro. (a) The expression level of hsa_circ_0008896 after si-circ_0008896 transfection was detected using quantitative PCR. (b) CCK8 assay was conducted to measure cell viability after down-regulation of hsa_circ_0008896. (c) The expression levels of two proliferation markers, Ki67 & PCNA after down-regulation of hsa_circ_0008896 were detected using Western blotting. (d) Colony formation assay was conducted to examine proliferation ability after down-regulation of hsa_circ_0008896. (e) The quantification results of (d). (f) Transwell migration & invasion assays were conducted to examine the migration & invasion abilities of VSMCs after down-regulation of hsa_circ_0008896. (g) The quantification results of (f). *P < 0.05, **P < 0.01, ***P < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35212610), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Ca, Dr, I, Po

Species Glossary

Reactivity: Hu, Mu, Rt, Ca, Dr, I, Po

Applications:

, , , , ,

Applications: , , , , ,

Host:

Goat Polyclonal

Host: Goat Polyclonal

Alt Catalog#

IMG-3073

Alt Catalog# IMG-3073

Conjugate:

Unconjugated

compare

(select up to 3 products from this page to compare)

AF5718

GAPDH Antibody [Unconjugated]

(4 Reviews)

(65 Publications)

100 μg

AF5718

HAF017). A specific band was detected for GAPDH/G3PDH at approximately 38 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2." class="big_lightbox">

Western blot shows lysates of mouse, human, and rat brain tissue. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human/Mouse/Rat GAPDH/G3PDH Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5718) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (<a class=

HAF017). A specific band was detected for GAPDH/G3PDH at approximately 38 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2." alt="Western blot shows lysates of mouse, human, and rat brain tissue. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human/Mouse/Rat GAPDH/G3PDH Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5718) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (HAF017). A specific band was detected for GAPDH/G3PDH at approximately 38 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2." class="big_thumb" />

NL001) and counterstained with DAPI (blue). View our protocol for Fluorescent ICC Staining of Cells on Coverslips." class="big_lightbox">

GAPDH was detected in immersion fixed HeLa human cervical epithelial carcinoma cell line using Goat Anti-Human/Mouse/Rat GAPDH Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5718) at 5 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Goat IgG Secondary Antibody (red; <a class=

NL001) and counterstained with DAPI (blue). View our protocol for Fluorescent ICC Staining of Cells on Coverslips." class="big_thumb" />

CTS008) and counterstained with hematoxylin (blue). Specific staining was localized to cytoplasm and nuclei of convoluted tubules. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.This application has not been tested in mouse or rat samples." class="big_lightbox">

GAPDH/G3PDH was detected in immersion fixed paraffin-embedded sections of normal human kidney using Goat Anti-Human/Mouse/Rat GAPDH/G3PDH Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5718) at 8 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; <a class=

CTS008) and counterstained with hematoxylin (blue). Specific staining was localized to cytoplasm and nuclei of convoluted tubules. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.This application has not been tested in mouse or rat samples." class="big_thumb" />

VC004). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to cytoplasm and nuclei. View our protocol for IHC Staining with VisUCyte HRP Polymer Detection Reagents." class="big_lightbox">

GAPDH was detected in immersion fixed paraffin-embedded sections of human prostate cancer tissue using Goat Anti-Human/Mouse/Rat GAPDH Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5718) at 3 µg/mL for 1 hour at room temperature followed by incubation with the Anti-Goat IgG VisUCyte™ HRP Polymer Antibody (<a class=

VC004). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to cytoplasm and nuclei. View our protocol for IHC Staining with VisUCyte HRP Polymer Detection Reagents." class="big_thumb" />

HAF109). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system." class="big_lightbox">

Simple Western lane view shows lysates of human brain (motor cortex) tissue and HepG2 human hepatocellular carcinoma cell line, loaded at 0.2 mg/mL. A specific band was detected for GAPDH at approximately 43 kDa (as indicated) using 10 µg/mL of Goat Anti-Human/Mouse/Rat GAPDH Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5718) followed by 1:50 dilution of HRP-conjugated Anti-Goat IgG Secondary Antibody (<a class=

HAF109). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system." class="big_thumb" />

<b>Biological Strategies Validation. </b>Role of Akt pathway in aliskiren's effects on attenuating collagen expression.A and B demonstrate the results of Western blotting for phospho- and total Akt in hearts of mice treated with various diets. C shows changes in the protein levels of collagen type I, phospho- and total Akt in response to 24 hours of exposure to D,L. Homocysteine (200 µmol/L) with or without pre-treatment with aliskiren 10 µmol/L (AL), wortmannin 1 µmol/L or Akt Inhibitor VIII 1 µmol/L. Hhe – Hhe-inducing diet; D,L, homocysteine (lower panel); AL 0.05– aliskiren 0.5 mg/kg/day; AL 5– aliskiren 5 mg/kg/day; AL 50– aliskiren 50 mg/kg/day; Wort – wortmannin; Akt in – Akt inhibitor VIII. *p<0.05; **p<0.01; and ***p<0.001. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24349097), licensed under a CC-BY license. Not internally tested by R&D Systems.

Effect of prodigiosins on the mRNA and protein expression of HO-1 in gastric tissue.Data (means ± SEM of three assays) were normalized to the levels of GAPDH and expressed as fold induction (log2 scale), relative to the level of HO-1 in the control. aP < 0.05, significant difference vs. the health rats; bP < 0.05, significant difference vs. HCl/ethanol-induced rats, Duncan's post-hoc test. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31194753), licensed under a CC-BY license. Not internally tested by R&D Systems.

The DU145FP cells express higher levels of cancer stemness related genes. (A) Transcriptome analyses of prostate cancer stemness-related markers. The Log2 transformed ratio of FPKM values (e.g., FP/WT) are indicated by color-coded index bars. (B) Cells were stained with fluorophore conjugated monoclonal antibodies against CD44 and EPCAM, the antibody against integrin alpha 2 beta 3 without fluorophore conjugation was detected by using secondary antibody conjugated with fluorophore, and stained cells were analyzed by flow cytometry. The scatter plots and histograms show representative results. CTRL denote cell stained with isotype control antibody or only secondary antibody; ST denote cell stained with antibody against EPCAM and integrin alpha 2 beta 3; US denote unstained cells. (C) Immunoblotting confirmation of the protein expression of A-tubulin, GAPDH, SOX9, SLUG, HIF1A, HIF2A, CD44 and integrin alpha 2 beta 3. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28698547), licensed under a CC-BY license. Not internally tested by R&D Systems.

<b>Biological Strategies Validation. </b>Effects of aliskiren on homocysteine-induced matrix expression in cultured cardiac fibroblasts.Fibroblasts were cultured in the presence or absence of D,L, homocysteine 200 µmol/L for 24 hours after pretreatment with varying concentrations of aliskiren (0.1–10 µmol/L). Real time PCR was done to measure relative expression of COLIA2 (alpha 2 chain of type I collagen; A) and COL3A1 (alpha 1 chain of type III collagen; B) genes. Figure 5C demonstrates the results of real time PCR to compare the effects of losartan and captopril with aliskiren on homocysteine induced expression of COL1A2 gene. Western blotting was conducted to measure the expression of collagen type I protein (D and E) Glyceraldehyde 3 phosphate dehydrogenase (GAPDH) was used as internal control. Hcy-D,L, homocysteine; AL-aliskiren; Los – losartan; and Cap – captopril. *p<0.05. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24349097), licensed under a CC-BY license. Not internally tested by R&D Systems.

Effects of aliskiren on myocardial matrix gene expression.Real time PCR was performed with ventricular tissue obtained from mice after 12-inducing diet and different doses of aliskiren. Figure 3A demonstrates changes in expression of COL1A1(alpha 1 chain of type I collagen) and 3B shows changes in COL1A2(alpha2 chain of type I collagen) genes. Lower right panels (3C and 3D) demonstrate the results of western blotting for collagen type I in various groups. Hhe – Hhe-inducing diet; AL 0.5– aliskiren 0.5 mg/kg/day; AL 5– aliskiren 5 mg/kg/day; and AL 50– aliskiren 50 mg/kg/day. * p<0.05; and *** p<0.001. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24349097), licensed under a CC-BY license. Not internally tested by R&D Systems.

S. Typhimurium evades autophagy by disrupting Sirt1-dependent AMPK activation.(A) Immunofluorescence image of S. Typhimurium co-localization with LC3 in GFP-LC3 expressing BMDMs at indicated time points. Data shown are representative of 3 independent experiments (n = 3). (B) Immunoblot analysis of p62 and LC3 expression upon S. Typhimurium infection in BMDMs. (C) LC3 and p62 expression levels are quantified by densitometry analysis. Data shown are from 3 independent experiments. (D) Confocal image of macrophages stained for Sirt1 and LC3. (E) BMDMs stained for LC3 and AMPK upon S. Typhimurium infection. (F) Confocal image of macrophages stained for LKB1 and LC3. (G) Immunoblot analysis of Sirt1, AMPK and LKB1 in wild type (WT) and Atg7-deficient macrophages. (H) Densitometric analysis of Sirt1, AMPK and LKB1 immunoblots (n = 3). Bar graphs are expressed as mean ± SEM, ***p≤0.001, **p≤0.01 and *p≤0.05. Scale bar = 10μm for microscopical images. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28192515), licensed under a CC-BY license. Not internally tested by R&D Systems.

$S. Typhimurium mediated targeting of Sirt1 for lysosomal degradation is virulence dependent.Immunoblot analysis of ACC and LKB1 activation upon infection with delta ssrB(A) and delta ssaV(B) compared to S. Typhimurium. Sirt1 and acetylated-NF kappa B from macrophages infected with delta ssrB(C)and delta ssaV(D) compared to S. Typhimurium. (E) Expression of Sirt1 from cytoplasmic (C) and nuclear (N) fraction from BMDMs infected with delta ssrB. (F) Confocal image of Sirt1 and LysoTracker Red in delta ssrB-infected BMDMs. Sirt1-LysoTracker Red co-localization in untreated BMDMs infected with S. Typhimurium for 4h is shown for comparison (n = 3). (G) Immunoblot analysis of LC3 and p62. (H) Densitometric analysis of LC3 lipidation and p62 (n = 4). (I) Immunofluorescence image of delta ssrB-infected BMDMs stained for LC3 and LPS of S. Typhimurium (n = 3). (J) Quantitation of LC3 co-localization with SCVs. 100 SCVs were counted and expressed as percentage co-localization. (K) AKT, mTOR, p70S6K, NDRG1 expression upon S. Typhimurium (ST) and delta ssrB infection in BMDMs. (L) Densitometric analysis of AKT, mTOR, p70S6K and NDRG1 are shown from 3 independent experiments. Bar graphs are expressed as mean ± SEM, ***p≤0.001. Scale bar = 10μm for microscopical images. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28192515), licensed under a CC-BY license. Not internally tested by R&D Systems.$

CD44bright cells are mainly positive for ABCG2, Oct3/4 and Nanog.(A) Double staining of CD44 and ABCG2 surface markers with flow cytometry assay shows higher levels expressions of these factors in both cell lines under hypoxia for 48 hours. (B) The CD44bright cells under normoxia express higher levels of ABCG2, Oct3/4 and Nanog, but the CD44dim cells under the same normoxia condition express very low levels of these factors. The CD44bright cells pretreated under 1% O2 for 48 hours show even higher levels of these factors compared to the CD44bright cells cultivated under normoxia. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/22216200), licensed under a CC-BY license. Not internally tested by R&D Systems.

Evaluation of ZL-2201 antiproliferative activity in vitro. A, Chemical structure of ZL-2201, a potent and selective DNA-PK inhibitor. B, Concentration-dependent response to ZL-2201 in M059J and M059K glioblastoma cancer cells measured by CTG after 6-day of treatment. The graph represents the average inhibitory (IC50) values (n = 3). C, Concentration-dependent response to ZL-2201 in CRISPR KO of ATM in A549 and FaDu cancer cells measured by CTG after 6 days of treatment. The graph represents the average inhibitory (IC50) values (n = 2–5). D, IC50 responses to ZL-2201 in ATM mutant cell lines (black bars) versus ATM WT A549 cell line (gray bar). Cell growth was measured by CTG after 6 days of treatment. The graph represents the average inhibitory (IC50) values (n = 2–6). NCI-H1703 (E) and A549 (F) cancer cells were treated with bleomycin (10 μmol/L) for 2 hours followed by the addition of increasing concentration of ZL-2201 for 2 hours. Whole-cell lysates were harvested, and concentration-dependent inhibition of DNA-PK protein were analyzed by Simple Western. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37663435), licensed under a CC-BY license. Not internally tested by R&D Systems.

Phenotypic evaluation of ZL-2201 synergy with various DNA-damaging agents. C, NCI-H1703 cells treated with ZL-2201 (0.1, 0.3, 0.5, 1,&3.6 μmol/L)&a low dose of doxorubicin (0.006 μmol/L) for 2 hours. Whole-cell lysates harvested,&Simple Western was used to show the inhibition of pDNA-PK upon combination treatment of ZL-2201 with doxorubicin. Image collected & cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37663435), licensed under a CC-BY license. Not internally tested by R&D Systems.

Reactivity:

Hu, Mu, Rt

Species Glossary

Reactivity: Hu, Mu, Rt

Applications:

, , ,

Applications: , , ,

Host:

Goat Polyclonal

Host: Goat Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	AF5718U-100UG
Alexa Fluor 405	AF5718V-100UG
Alexa Fluor 488	AF5718G-100UG
Alexa Fluor 532	AF5718X-100UG
Alexa Fluor 594	AF5718T-100UG
Alexa Fluor 647	AF5718R-100UG
Alexa Fluor 700	AF5718N-100UG
Alexa Fluor 750	AF5718S-100UG
Alexa Fluor Plus 405	AF5718AFP405-100UG
Alexa Fluor Plus 488	AF5718AFP488-100UG
Alexa Fluor Plus 555	AF5718AFP555-100UG
Alexa Fluor Plus 594	AF5718AFP594-100UG
Alexa Fluor Plus 647	AF5718AFP647-100UG
Alexa Fluor Plus 680	AF5718AFP680-100UG
Allophycocyanin	AF5718A
Biotin	AF5718B
CoraFluor 1	AF5718CL1
DyLight 350	AF5718D
DyLight 405	AF5718E
DyLight 488	AF5718K
DyLight 550	AF5718L
DyLight 594	AF5718M
DyLight 650	AF5718W
DyLight 680	AF5718Y
DyLight 755	AF5718Z
FITC	AF5718F
HRP	AF5718H
Janelia Fluor 525	AF5718JF525
Janelia Fluor 549	AF5718I
Janelia Fluor 646	AF5718J
Janelia Fluor 669	AF5718JF669
PE	AF5718P
PerCP	AF5718C
mFluor Violet 450 SE	AF5718MFV450
mFluor Violet 500 SE	AF5718MFV500
mFluor Violet 610 SE	AF5718MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
Carrier Free	AF5718-SP

compare

(select up to 3 products from this page to compare)

NB300-327

GAPDH Antibody

(3 Reviews)

(57 Publications)

0.1 ml

NB300-327

Western Blot: GAPDH Antibody [NB300-327] - Theoretical molecular weight: 36 kDa. Detection of GAPDH in mouse liver.

Western Blot: GAPDH Antibody [NB300-327] - Western blot analysis of extracts from Jurkat and HeLa cells using NB300-327 at 1:1000. Theoretical molecular weight: 36 kDa.

$Western Blot: GAPDH Antibody [NB300-327] - Analysis of different cell cytosolic or nuclear enriched fractions, GAPDH antibody, dilution 1:20,000 (Red): [1] protein standard, [2] NIH-3T3 cytosolic, [3] NIH-3T3 nuclear, [4] HeLa cytosolic, and [5] HeLa nuclear fractions. Strong band at 37kDa corresponds to GAPDH protein, mainly detected in the cytosolic fractions. The same blot was simultaneously probed with mouse mAb to the nuclear RNA binding protein SF3B4, dilution 1:1,000 (Green). In contrast to GAPDH, SF3B4 is exclusively expressed in the nuclear fraction.$

Immunocytochemistry/Immunofluorescence: GAPDH Antibody [NB300-327] - The GAPDH antibody was tested in Hela cells at a 1:500 dilution against Dylight 488 (Green). Alpha-tubulin and nuclei were counterstained with Dylight 550 (Red) and DAPI (Blue), respectively.

Immunocytochemistry/Immunofluorescence: GAPDH Antibody [NB300-327] - Confocal immunofluorescence analysis of HeLa cells using GAPDH (NB300-327) antibody (green). Nuclei was counterstained with DAPI (blue).

Immunocytochemistry/Immunofluorescence: GAPDH Antibody [NB300-327] - IF Confocal analysis of C2C12 cells using GAPDH antibody (NB300-327, 1:20). An Alexa Fluor 488-conjugated Goat to rabbit IgG was used as secondary antibody (green). Actin filaments were labeled with Alexa Fluor 568 phalloidin (red). DAPI was used to stain the cell nuclei (blue).

Simple Western: GAPDH Antibody [NB300-327] - Simple Western lane view shows a specific band for GAPDH in 0.2 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system. Note: band observed higer than predicted 36 kDa molecular weight.

nb300-327_rabbit-polyclonal-gapdh-antibody-25520231539521.jpg

Representative immunoblot of KDR and FGFR CAM protein expression levels examined by Western blotting. GNS, graphene nanosheet; NG, graphite nanoparticle; ND, diamond nanoparticle; C60, fullerene C60; MWNT, multi-wall nanotube; KDR, vascular endothelial growth factor receptor; FGFR, fibroblast growth factor receptor; GAPDH, glyceraldehyde-3-phosphate dehydrogenase.

Western Blot: GAPDH Antibody [NB300-327] - Increased PIP expression in the lungs of PF‐PH compared to PF ratsA, BRelative expression of PIP mRNA (A) & protein (B) normalized to GAPDH.CRepresentative images & PIP quantification.Data information: Values are expressed as mean ± SEM. The number of samples per group for each experiment is included within each bar graph (t‐test; *P < 0.05, **P < 0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31468711), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Western Blot: GAPDH Antibody [NB300-327] - Effects of subchronic administration (7 & 14 days) of therapeutic relevant concentration of Brex (Brex: 300 nM) & interaction between Brex & 5-HT1A receptor (5-HT1AR) antagonist WAY100635 (WAY: 10 μM) on protein expression of 5-HT1A (panel A) & 5-HT7 (panel B) receptor in the plasma membrane fraction of cortical primary cultured astrocytes. In left side histograms, ordinate: mean ± SD (n = 6) of the relative protein level of 5-HT1AR & 5-HT7R per GAPDH. * p < 0.05, ** p < 0.01: relative to control (Brex-free) by one-way analysis of variance (ANOVA) with Tukey’s post-hoc test, & @ p < 0.05: relative to Brex for 14 days by Student’s T-test. Right side panels indicate their pseudo-gel images using capillary immunoblotting. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35743014), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: GAPDH Antibody [NB300-327] - Online lung microarray analysis revealed PIP as one of the Slug transcriptional targets mediating vascular cell proliferation in PF‐PHAHeatmap of the 20 genes upregulated in GSE24988 microarray & known to be Slug transcriptional target.BVenn diagram showing the overlap between Slug targets implicated in cell proliferation & known to be extracellular.CHeatmap of the seven transcriptional targets of Slug known to promote proliferation & to be extracellular.D, ERelative expression of prolactin‐induced protein (PIP) mRNA (D) & protein (E) expression normalized to GAPDH in PF & PF‐PH patients.FRepresentative images of PIP immunohistochemistry showing its extracellular localization & quantification.G–JProliferation assay on healthy fibroblast (G), pulmonary arterial EC (H), & healthy pulmonary arterial SMC (I & J) in the presence or absence of PIP.Data information: Values are expressed as mean ± SEM. The number of samples per group for each experiment is included within each bar graph. Statistical test: panels (D–F): t‐test; panels (G–J): ANOVA (*P < 0.05, **P < 0.01 ***P < 0.001). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31468711), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody [NB300-327] - Growth of lactobacilli on IECs & their influence towards C. albicans cytotoxicity, adhesion, hyphal length & translocation. (A) LDH release of IECs colonized (Pre-Inc.) or simultaneously colonized (w/o Pre-Inc.) with L. rhamnosus (L.r.) at different MOI (5, 50 or 250) & infected or not with C. albicans (C.a.) (MOI 1) & measured at 24 h post-infection. (B) Growth of L. paracasei (L.p.), L. rhamnosus, L. salivarius (L.s.), L. fermentum (L.f.), & L. brevis (L.b.) on IECs. (C) Percentage of C. albicans adhered to IECs colonized with different Lactobacillus species (MOI 50) at 1 h post-infection. (D) C. albicans hyphal induction on IECs or on plastic colonized with L. rhamnosus or L. brevis (MOI 50) at 4 h post-infection. Results were normalized to C. albicans single infection. (E) Translocation of C. albicans (MOI 1) across IECs colonized with L. rhamnosus or L. brevis (MOI 50) at 24 h post-infection. (F) Assessment of epithelial barrier integrity measured as the loss of transepithelial electrical resistance (TEER) in response to L. rhamnosus or L. brevis (MOI 50) colonization & C. albicans infection in the presence or absence of Lactobacillus colonization at 24 h post-infection. Data are TEER loss in percentage of uninfected host cells (before pre-incubation). (G) E-Cadherin protein expression analyzed by western blot compared to GAPDH in IECs that were left uninfected or colonized with L. rhamnosus (MOI 50) & infected with C. albicans for 6, 12 & 24 h. Data are mean±s.e.m. *P<0.05, **P<0.01, ***P<0.005 (t-test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31413153), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Panel (D) indicates the expression of connexin43 (Cx43) and pannexin1 (PANX1) in the plasma membrane fraction of the PPN between wild type (grey columns) and S286L-TG (black columns). Ordinates indicate the mean � SD (n = 6) of the relative expression of connexin43 and pannexin1 per GAPDH. Right-side panels indicate the pseudo-gel images of connexin43, pannexin1 and GAPDH, obtained using capillary immunoblotting. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/40564986/), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Reactivity:

Hu, Mu, Rt, Po, Ba, Bv, Ch, Eq, Fu, In, Ye

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Ba, Bv, Ch, Eq, Fu, In, Ye

Applications:

, , ,

Applications: , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

compare

(select up to 3 products from this page to compare)

NB300-322

GAPDH Antibody

(2 Reviews)

(44 Publications)

0.1 ml

NB300-322

Immunohistochemistry: GAPDH Antibody [NB300-322] - Detection of human GAPDH by immunohistochemistry. Sample: FFPE section of human colon carcinoma. Antibody: Affinity purified rabbit anti-GAPDH (NB300-322). Detection: DAB

Immunocytochemistry/Immunofluorescence: GAPDH Antibody [NB300-322] - GAPDH detection in HeLa cells with ICC-IF application using NB300-322, visualized with DyLight Fluor 488.

Immunohistochemistry: GAPDH Antibody [NB300-322] - Detection of mouse GAPDH by immunohistochemistry. Sample: FFPE section of mouse plasmacytoma. Antibody: Affinity purified rabbit anti-GAPDH (NB300-322). Detection: DAB

Western Blot: GAPDH Antibody [NB300-322] - Mouse DRG stained at 1:2000 dilution. Image provided by verified customer review.

Immunohistochemistry-Paraffin: GAPDH Antibody [NB300-322] - IHC-P detection of GAPDH in formalin fixed paraffin embedded section of human lung carcinoma using NB300-322 at a dilution of 1:200.

Immunohistochemistry-Paraffin: GAPDH Antibody [NB300-322] - IHC-P detection of GAPDH in formalin fixed paraffin embedded section of mouse squamous cell carcinoma using NB300-322 at a dilution of 1:200.

$Time-dependent effects of subacute administration of effective dose of escitalopram (5 mg/kg/day) for 3 & 7 days on expression of 5-HT7R in the thalamic plasma membrane fraction (Panel (A)). Ordinate: mean ± SD (n = 6) of the relative protein level of 5-HT7R in the thalamic plasma membrane fraction. Panel (B) indicates the pseudo-gel images using capillary immunoblotting. ** p < 0.01 vs. control by one-way analysis of variance with Tukey’s post-hoc test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33572981), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

$Western Blot: GAPDH Antibody [NB300-322] - Concentration-dependent effects of subchronic administration of ZTP on Cx43 protein expression in the plasma membrane fraction (A) & their pseudogel images, using capillary immunoblotting (B). Ordinate: mean ± SD (n = 6) of the relative protein level of Cx43 (per GAPDH). Concentration-dependent effects of ZTP (100, 300 & 1000 nM) on Cx43 expression in the plasma membrane fraction of the primary cultured astrocytes were analysed by one-way ANOVA with Tukey’s (wholly significant difference) post hoc test (** p < 0.01 vs. ZTP free (0)). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/34832898), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

$Western Blot: GAPDH Antibody [NB300-322] - Concentration-dependent effects of subchronic administration of ZTP on Cx43 protein expression in the cytosol fraction (A) & their pseudogel images, using capillary immunoblotting (B). Ordinate: mean ± SD (n = 6) of the relative protein level of Cx43 (per GAPDH). Concentration-dependent effects of ZTP (100, 300 & 1000 nM) on Cx43 expression in the cytosol fraction of the primary cultured astrocytes were analysed by one-way ANOVA with Tukey’s (wholly significant difference) post hoc test (* p < 0.05 vs. ZTP free (0)). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/34832898), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

$Western Blot: GAPDH Antibody [NB300-322] - Effects of acute (120 min) administration of supratherapeutic concentration of ZTP (1000 nM) & chronic (14 days) administration of therapeutically relevant concentrations of ZTP (300 nM) on Cx43 protein expression in the plasma membrane fraction (A) & their pseudogel images, using capillary immunoblotting (B). Ordinate: mean ± SD (n = 6) of the relative protein level of Cx43 (per GAPDH). Effects of ZTP on Cx43 expression in the plasma membrane fraction of the primary cultured astrocytes were analysed by student T-test (* p < 0.05 vs. control: ZTP free). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/34832898), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

$Western Blot: GAPDH Antibody [NB300-322] - Interaction between subchronic administration of supratherapeutic concentration of ZTP & Akt inhibitor (DEBC) on Cx43 protein expression in the astroglial plasma membrane fraction (A) & their pseudogel images, using capillary immunoblotting (B). Ordinate: mean ± SD (n = 6) of the relative protein level of Cx43 (per GAPDH). Effects of ZTP (1000 nM) & Akt inhibitor (DEBC: 10 μM) on Cx43 expression in the plasma membrane fraction of the primary cultured astrocytes were analysed by two-way ANOVA with Tukey’s (wholly significant difference) post hoc test (** p < 0.01 vs. control, @@ p < 0.01 vs. non). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/34832898), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

$Simple Western: GAPDH Antibody [NB300-322] - Effects of subchronic nicotine administration on the expression of phosphorylated protein kinase B (pAkt) & phosphorylated extracellular signal-regulated kinase (pErk) in the plasma membrane fraction of OFC. Effects of the systemic subchronic administration of nicotine (50 mg/kg/day for seven days) on pAkt & pErk expression in the OFC plasma membrane fraction before four week of age (A,C) & after 12 week of age (B,D), ADSHE onset of the wild-type & S286L-TG & pseudo-gel images, using capillary immunoblotting. Ordinate: mean ± SD (n = 6) of the relative protein level of pErk & pAkt. * p < 0.05, ** p < 0.01 vs. wild-type, & @ p < 0.05, @@ p < 0.01 vs. nicotine-free (non) by two-way ANOVA with Tukey’s multiple comparison. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33143372), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

$Simple Western: GAPDH Antibody [NB300-322] - Effects of the subacute administration of effective doses of vortioxetine (2.5 mg/kg/day), escitalopram (5 mg/kg/day), & lurasidone (3 mg/kg/day) for 3 days on the expression of 5-HT7R in the thalamic plasma membrane fraction (Panel (A)). Ordinate: mean ± SD (n = 6) of the relative protein level of 5-HT7R in the thalamic plasma membrane fraction. Panel (B) indicates the pseudo-gel images using capillary immunoblotting. * p < 0.05, ** p < 0.01 vs. the control by Student’s t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33572981), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: GAPDH Antibody [NB300-322] - Gem expression is sufficient to increase cell motility.(A): HeLa cells were transduced with Lenti-control or Lenti-Tax viral particles. When cells reached 100% confluence, a wound was made in the cell monolayer & pictures were taken at 0 h & up to 12 h post-wounding. Measurements between the 2 fronts of migration were performed using image-J software (NIH, USA). (B): Percentage of healing during a 12 h kinetic. (C): Western blot analyses were performed on 70 µg of cellular extracts transduced by Lenti-control or Lenti-Tax viral particles. Membranes were probed with anti-Gem (1∶2,000) or anti-GAPDH (1∶1,000) antibody. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.ppat.1003917), licensed under a CC0-1.0 license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody [NB300-322] - Gem expression is sufficient to increase chemokinesis & chemotaxis.(A, C): MOLT4 cells were transduced with Lenti-control or Lenti-GEM. Forty-eight hours later, 5.105 cells were collected & loaded on a 5 µm permeable Transwell filter in absence or presence of SDF1/CXCL12 (150 ng/ml). Twenty-four hours later, cell migration was quantified by flow cytometry (flow cytometer Facscalibur4c+HTS (BD biosciences)). (B, D): Western blot analyses were performed on 70 µg of cellular extracts from MOLT4 cells transduced by Lenti-control or Lenti-GEM viral particles. Membranes were probed with anti-Gem (1∶2,000) or anti-GAPDH (1∶1,000) antibody. ***: significantly different, p<0.0001, Student's t-test. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.ppat.1003917), licensed under a CC0-1.0 license. Not internally tested by Novus Biologicals.

$Western Blot: GAPDH Antibody [NB300-322] - Effects of subchronic administration of therapeutic-relevant concentration of antipsychotics, CLZ (3 μM), QTP (1 μM) & BPZ (0.3 μM), on Cx43 protein expression in the plasma fraction (A) & their pseudo-gel images, using capillary immunoblotting (B). Ordinate: mean ± SD (n = 6) of the relative protein level of Cx43 (per GAPDH). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/34070699), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

$Western Blot: GAPDH Antibody [NB300-322] - Interaction between acute administration of therapeutic-relevant concentration of antipsychotics & Akt inhibitor (DEBC) on Cx43 protein expression in the astroglial plasma membrane fraction, after subchronic administration of therapeutic-relevant concentration of VPA (500 μM) (A). Interaction between subchronic administration of therapeutic-relevant concentration of antipsychotics & DEBC on Cx43 protein expression in the astroglial plasma membrane fraction, after subchronic administration of therapeutic-relevant concentration of VPA (B). Lower panels indicate their pseudo-gel images, using capillary immunoblotting. Ordinate: mean ± SD (n = 6) of the relative protein level of Cx43 (per GAPDH). Effects of antipsychotics & Akt inhibitor (DEBC: 10 μM) on Cx43 expression in the plasma membrane fraction of the primary cultured astrocytes were analyzed by MANOVA with Tukey’s post hoc test (** p < 0.01 vs. non, @@ p < 0.01 vs. control). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/34070699), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: GAPDH Antibody [NB300-322] - Gem is overexpressed in T- & non-T-Tax-expressing cells as well as in HTLV-1 infected cells.(A): Total RNA was extracted from 293T cells transduced with Lenti-control (lane 2) or Lenti-Tax (lane 3) & RT-PCR was performed using gem or GADPH specific primers. Lane 1 is a control of extraction. (B, C): Western blot analyses were performed with 70 µg of proteins from (B) 293T or (C) MOLT4 cells transduced by Lenti-control or Lenti-Tax vectors (72 h post-transduction). (D): JPX-9 cells were grown for 24 h or 48 h in the presence of ZnCl2 (120 µM). Western blot analyses were performed with 70 µg of JPX-9 cellular extracts. (E): Western blot analyses were performed with 70 µg of cellular extracts obtained from non-infected (CEM, Jurkat & MOLT4) or HTLV-1-infected (C8166, C91/PL, Hut102 & MT2) T-lymphocytes. (B, C, D, E): Membranes were probed with anti-Gem (1∶2,000) & anti-GAPDH (1∶1,000) or anti-Tax Tab 172 (1∶500) antibodies. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.ppat.1003917), licensed under a CC0-1.0 license. Not internally tested by Novus Biologicals.

$Simple Western: GAPDH Antibody [NB300-322] - Age-dependent fluctuations of pannexin1 expression in the plasma membrane in OFC of wild type and S286L-TG. Panel (A) indicates expressions of pannexin1 in the plasma mem-brane fraction of OFC of wild type (brown columns) and S286L-TG (green columns) at 4, 7, and 10 weeks of age, respectively. Ordinates indicate the mean ± SD (n = 6) of relative expression of pannexin1 per GAPDH, and abscissas indicate ages (weeks). ** p < 0.01, relative to pannexin1 expression at 4 weeks of age, @@ p < 0.01, relative to the wild type of the same age using two-way ANOVA with Scheffe’s post hoc test. F value was [Fage(2,30) = 0.7 (p > 0.1), Fgenotype(1,30) = 30.7 (p < 0.01), Fage*genotype(2,30) = 11.0 (p < 0.01)]. Panel (B) indicates the pseudo-gel images of pannexin1 and GAPDH using capillary immunoblotting. Image collected and cropped by CiteAb under a CC-BY license from the following publication: Age-Dependent Activation of Pannexin1 Function Contributes to the Development of Epileptogenesis in Autosomal Dominant Sleep-related Hypermotor Epilepsy Model Rats. <i>Int J Mol Sci</i> (2024). Not internally tested by Novus Biologicals.$

$Simple Western: GAPDH Antibody [NB300-322] - Astroglial expression in the plasma membrane evoked by ripple burst and fast ripple burst stimulations in wild type and S286L-TG. Panel (A) indicates expression of pannexin1 in the astroglial plasma membrane fraction. Ordinates indicate the mean ± SD (n = 6) of relative expression of pannexin1 per GAPDH. Gray and green bars indicate pannexin1 expression in astrocytes of wild type and S286L-TG after chronic fast ripple-evoked stimulation, respectively. * p < 0.05, ** p < 0.01 using two-way ANOVA with Scheffe’s post hoc test. F value was [Fgenotype(1,20) = 16.6 (p < 0.01), Fage(1,20) = 2.0 (p > 0.1), Fgenotype*age(1,20) = 5.4 (p < 0.05)]. Panel (B) indicates the pseudo-gel images of P2X7R and GAPDH, using capillary immunoblotting. Image collected and cropped by CiteAb under a CC-BY license from the following publication: Age-Dependent Activation of Pannexin1 Function Contributes to the Development of Epileptogenesis in Autosomal Dominant Sleep-related Hypermotor Epilepsy Model Rats. <i>Int J Mol Sci</i> (2024). Not internally tested by Novus Biologicals.$

Reactivity:

Hu, Mu, Rt, Ch, Pm, Po, Am, Av, Bv, Ca, ChHa, Ma, Fi, SyHa, Gp, Ha, Rb, Sh, Sq, Tr, Xp, Ze

Species Glossary

Reactivity: Hu, Mu, Rt, Ch, Pm, Po, Am, Av, Bv, Ca, ChHa, Ma, Fi, SyHa, Gp, Ha, Rb, Sh, Sq, Tr, Xp, Ze

Applications:

, , , , ,

Applications: , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Conjugate:

Unconjugated

compare

(select up to 3 products from this page to compare)

NBP2-27103

GAPDH Antibody (13H12) - BSA Free

(3 Reviews)

(38 Publications)

0.1 mg

NBP2-27103

Immunohistochemistry-Paraffin: GAPDH Antibody (13H12) [NBP2-27103] - IHC-P detection GAPDH protein in a formalin-fixed paraffin-embedded section of human rectal carcinoma tissue using GAPDH antibody (clone 13H12) at 5 ug/ml concentration.

<b>Biological Strategies Validation. </b>Western Blot: GAPDH Antibody (13H12) [NBP2-27103] - Characterization of lncR492.(B) Northern blot of lncR494 using increasing amounts of loaded total. Black arrow signifies lncR492-specific signal at approximately 1400 bp. A probe targeting Gapdh mRNA served as the loading control. (D) RT-PCR analysis of lncR492 and Gapdh expression. RNA extract was treated with a 5'-phosphate-dependent exonuclease, resulting in a degradation of f.ex. ribosomal RNA.Citation: Winzi M, Casas Vila N, Paszkowski-Rogacz M, Ding L, Noack S, Theis M, et al. (2018) The long noncoding RNA lncR492 inhibits neural differentiation of murine embryonic stem cells. PLoS ONE 13(1): e0191682. //doi.org/10.1371/journal.pone.0191682

GAPDH-Antibody-13H12-Western-Blot-NBP2-27103-img0018.jpg

Western Blot: GAPDH Antibody (13H12) [NBP2-27103] - WB detection of GAPDH protein (theoretical molecular weight 36 kDa) in lysates of Mouse cell lines (A) NIH 3T3 (B) RAW 264.7 using GAPDH antibody (clone 13H12) at a concentration of 0.25 ug/ml.

Western Blot: GAPDH Antibody (13H12) [NBP2-27103] - analysis of GAPDH in HeLa and HEK 293 cells (25ug/lane) using anti-GAPDH antibody. Image from verified customer review.

Immunohistochemistry-Paraffin: GAPDH Antibody (13H12) [NBP2-27103] - IHC-P detection GAPDH protein in a formalin-fixed paraffin-embedded tissue section of human esophageal squamous cell carcinoma (SCC) using GAPDH antibody (clone 13H12) at 5 ug/ml concentration.

Simple Western: GAPDH Antibody (13H12) [NBP2-27103] - GAPDH/G3PDH Antibody (13H12) [NBP2-27103] - Simple Western lane view shows a specific band for GAPDH in 0.1 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.

Western Blot: GAPDH Antibody (13H12) - BSA Free [NBP2-27103] - Effect of AAT on Mcl-1 phosphorylation, the activity of MAP kinases & caspases.Neutrophils from healthy volunteers (2.5 × 106/ml) were cultured in medium supplemented with patient serum (3 mg protein/ml; 1%) & those containing low levels of AAT (AAT-reduce serum; 1%) in the presence of STS (0.2 μM). After 3 h, the expression of pMcl-1 (A, n = 7), pAkt (B, n = 8) & pERK1/2 (C, n = 10) were analyzed by western blot. Expression levels of the phosphorylated proteins were normalized to that of the unphosphorylated forms. GAPDH was used as loading control. One representative blot is displayed. *p<0.05; **p<0.01; n.s. = not significant. D. After 4 h of incubation the activities of caspase-9 & caspase-3/-7 were quantified. Results are presented as means ± SEM of eight independent experiments. No significant differences were found (one-way ANOVA with Newman keuls post-hoc test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28493974), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Dr, Pm, Pm, Sh, Po, Bv, Ca, Ma, Gp, Re, Sq

Species Glossary

Reactivity: Hu, Mu, Rt, Dr, Pm, Pm, Sh, Po, Bv, Ca, Ma, Gp, Re, Sq

Applications:

, , ,

Applications: , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Alt Catalog#

IMG-6665A

Alt Catalog# IMG-6665A

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NBP2-27103AF350
Alexa Fluor 405	NBP2-27103AF405
Alexa Fluor 488	NBP2-27103AF488
Alexa Fluor 532	NBP2-27103AF532
Alexa Fluor 594	NBP2-27103AF594
Alexa Fluor 647	NBP2-27103AF647
Alexa Fluor 700	NBP2-27103AF700
Alexa Fluor 750	NBP2-27103AF750
Alexa Fluor Plus 405	NBP2-27103AFP405
Alexa Fluor Plus 488	NBP2-27103AFP488
Alexa Fluor Plus 555	NBP2-27103AFP555
Alexa Fluor Plus 594	NBP2-27103AFP594
Alexa Fluor Plus 647	NBP2-27103AFP647
Alexa Fluor Plus 680	NBP2-27103AFP680
Allophycocyanin	NBP2-27103APC
Biotin	NBP2-27103B
CoraFluor 1	NBP2-27103CL1
DyLight 350	NBP2-27103UV
DyLight 405	NBP2-27103V
DyLight 488	NBP2-27103G
DyLight 550	NBP2-27103R
DyLight 594	NBP2-27103DL594
DyLight 650	NBP2-27103C
DyLight 680	NBP2-27103FR
DyLight 755	NBP2-27103IR
FITC	NBP2-27103F
HRP	NBP2-27103H
Janelia Fluor 525	NBP2-27103JF525
Janelia Fluor 549	NBP2-27103JF549
Janelia Fluor 646	NBP2-27103JF646
Janelia Fluor 669	NBP2-27103JF669
PE	NBP2-27103PE
PerCP	NBP2-27103PCP
mFluor Violet 450 SE	NBP2-27103MFV450
mFluor Violet 500 SE	NBP2-27103MFV500
mFluor Violet 610 SE	NBP2-27103MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NBP2-27103SS
Azide and BSA Free	NBP2-80749

compare

(select up to 3 products from this page to compare)

MAB5718

GAPDH Antibody (686613) [Unconjugated]

(1 Review)

(43 Publications)

100 μg

MAB5718

HAF007). A specific band was detected for GAPDH/G3PDH at approximately 39 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2." class="big_lightbox">

Western blot shows lysates of human brain tissue, mouse brain tissue, and rat brain tissue. PVDF Membrane was probed with 0.05 µg/mL of Mouse Anti-Human/Mouse/Rat GAPDH/G3PDH Monoclonal Antibody (Catalog # MAB5718) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # <a class=

HAF007). A specific band was detected for GAPDH/G3PDH at approximately 39 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2." alt="Western blot shows lysates of human brain tissue, mouse brain tissue, and rat brain tissue. PVDF Membrane was probed with 0.05 µg/mL of Mouse Anti-Human/Mouse/Rat GAPDH/G3PDH Monoclonal Antibody (Catalog # MAB5718) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). A specific band was detected for GAPDH/G3PDH at approximately 39 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2." class="big_thumb" />

NL007) and counterstained with DAPI (blue). View our protocol for Fluorescent ICC Staining of Cells on Coverslips." class="big_lightbox">

GAPDH was detected in immersion fixed HeLa human cervical epithelial carcinoma cell line using Mouse Anti-Human/Mouse/Rat GAPDH Monoclonal Antibody (Catalog # MAB5718) at 8 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Mouse IgG Secondary Antibody (red; Catalog # <a class=

NL007) and counterstained with DAPI (blue). View our protocol for Fluorescent ICC Staining of Cells on Coverslips." class="big_thumb" />

CTS013). Tissue was stained using the Anti-Mouse HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS002) and counterstained with hematoxylin (blue). Specific staining was localized to cytoplasm and nuclei. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections." class="big_lightbox">

GAPDH/G3PDH was detected in immersion fixed paraffin-embedded sections of human kidney using Mouse Anti-Human/Mouse/Rat GAPDH/G3PDH Monoclonal Antibody (Catalog # MAB5718) at 15 µg/mL overnight at 4 °C. Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using Antigen Retrieval Reagent-Basic (Catalog # <a class=

CTS013). Tissue was stained using the Anti-Mouse HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS002) and counterstained with hematoxylin (blue). Specific staining was localized to cytoplasm and nuclei. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections." class="big_thumb" />

Simple Western lane view shows lysates of Jurkat human acute T cell leukemia cell line and C2C12 mouse myoblast cell line, loaded at 0.2 mg/mL. A specific band was detected for GAPDH/G3PDH at approximately 41 kDa (as indicated) using 0.25 µg/mL of Mouse Anti-Human/Mouse/Rat GAPDH/G3PDH Monoclonal Antibody (Catalog # MAB5718). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.

Simple Western lane view shows lysates of Jurkat human acute T cell leukemia cell line, HeLa human cervical epithelial carcinoma cell line, C2C12 mouse myoblast cell line, and C6 rat glioma cell line, loaded at 0.2 mg/mL. A specific band was detected for GAPDH at approximately 42 kDa (as indicated) using 1 µg/mL of Mouse Anti-Human/Mouse/Rat GAPDH Monoclonal Antibody (Catalog # MAB5718) . This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.

Simultaneous knockdown of multiple genes in primary human islets following electroporation. (A) Graph shows RT-qPCR results of islets electroporated with non-targeting control siRNA or siRNA targeting RB and p130 (L-003299). (B) Graph shows RT-qPCR results of islets electroporated with non-targeted control siRNA or siRNAs targeting the indicated gene products. The housekeeping gene GAPDH was used as the control. Representative experiment shown from 3 separate experiments. Error bars indicate standard deviation. (C) Western blot for RB protein in human islet lysates after electroporation of control or targeting siRNA. GAPDH was used as a loading control. RB appears as a characteristic doublet representing the hypo and hyperphosphorylated protein. Representative experiment shown from 3 different experiments. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/25305068), licensed under a CC-BY license. Not internally tested by R&D Systems.

Evaluation of CPP/mRNA-mediated protein expression. (A) Representative fluorescence images and a quantitative graph showing mCherry-positive CT26.CL25 cells 24 h after treatment with CPP/mCherry mRNA complexes (6.8 nM). Scale bar: 275 μm. Data are presented as the mean ± SD (n = 3). (B) Representative flow cytometry histograms and graphs of EGFP-positive CL26.CL25 cells transfected with CPP/EGFP mRNA complexes (6.8 nM). Data are presented as the mean ± SD (n = 3). (C) Western blot analysis of the expression levels of OVA and GAPDH in CT26.CL25 cells. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35745843), licensed under a CC-BY license. Not internally tested by R&D Systems.

Molecular effect of intraluminal chloride and GsMTx4 in smooth muscle cells. a-c Upper panel represents the main cumulative effect of intraluminal chloride concentration ([Cl−]) and medium supplementation with and without GsMTx4. a Examples of representative blots are shown. b, c Protein expression levels for b myosin light chain 2 (MLC2), and c alpha-smooth muscle actin ( alpha -SMA) are quantified. d–f Lower panel shows the additional effect of PIEZO1/2 inhibition after intraluminal injection of Cl− channels inhibitors: cystic fibrosis transmembrane conductance regulator inhibitor172 (CFTRinh) to CFTR and; calcium-dependent Cl− channel inhibitor A01 (CaCCinh) to CaCCs. d Examples of representative blots are shown. e–f Relative expression levels of e MLC2, and f alpha -SMA are displayed. 143 mM Cl− and standard solution (SS) represent the control condition for [Cl−] and Cl− channels inhibitors, respectively. White and dotted rectangles represent the medium supplementation with and without GsMTx4, respectively. Each lane represents a pooled-tissue sample, and the relative expression levels were determined against GAPDH. n ≥ 4 were used per antibody/condition. Results are presented as mean ± SD. Symbols indicate the main effects and non-redundant interactions of the two-way ANOVA. p < alpha 0.0001, beta 0.001, gamma 0.01, µ0.05 Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/36740669), licensed under a CC-BY license. Not internally tested by R&D Systems.

The impact of combination therapy on protein and gene expression in SJSA-1 osteosarcoma cells. (A) A Western blot analysis illustrating the effects of the combination treatment on key proteins involved in metastasis, cell survival, and apoptosis in SJSA-1 osteosarcoma cells. The expression levels of MMP9 and MMP13, which facilitate tumor cell invasion and metastasis through ECM degradation, were significantly reduced, indicating a potential inhibitory effect of the combination therapy on metastatic progression. Additionally, phosphorylated AKT (pAKT), a central regulator of the PI3K/AKT pathway associated with cell survival and chemoresistance, and runt-related transcription factor 2 (RUNX2), a critical modulator of osteosarcoma progression and tumor aggressiveness, were both downregulated, suggesting the suppression of key oncogenic pathways. Conversely, apoptotic markers, including cleaved caspase-8, cleaved caspase-3, and total caspase-3, exhibited increased activation following treatment, indicating enhanced apoptotic signaling. GAPDH was used as a loading control to ensure equal protein loading across samples. (B) A densitometric analysis of the Western blot bands representing the expression levels of target proteins after 48 h of treatment. The band intensities were quantified using Image Lab software (Version 6.1.0 build 7) and normalized to the GAPDH. Relative protein expression levels are expressed as a fold change compared to the untreated control group. The data represent the mean ± the standard deviation from two independent experiments. (C) qRT-PCR analyzed the gene expression of the apoptosis-related markers p16 and p53 following treatment. The results highlight the upregulation of p16 and stable expression of p53 in treated cells. (* p < 0.05 and ** p < 0.01). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/40332124), licensed under a CC-BY license. Not internally tested by R&D Systems.

Reactivity:

Hu, Mu, Rt

Species Glossary

Reactivity: Hu, Mu, Rt

Applications:

, , ,

Applications: , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	FAB5718U-100UG
Alexa Fluor 405	FAB5718V-100UG
Alexa Fluor 488	FAB5718G-100UG
Alexa Fluor 532	FAB5718X-100UG
Alexa Fluor 594	FAB5718T-100UG
Alexa Fluor 647	FAB5718R-100UG
Alexa Fluor 700	FAB5718N-100UG
Alexa Fluor 750	FAB5718S-100UG
Alexa Fluor Plus 405	FAB5718AFP405-100UG
Alexa Fluor Plus 488	FAB5718AFP488-100UG
Alexa Fluor Plus 555	FAB5718AFP555-100UG
Alexa Fluor Plus 594	FAB5718AFP594-100UG
Alexa Fluor Plus 647	FAB5718AFP647-100UG
Alexa Fluor Plus 680	FAB5718AFP680-100UG
Allophycocyanin	FAB5718A
Biotin	FAB5718B
CoraFluor 1	FAB5718CL1
DyLight 350	FAB5718D
DyLight 405	FAB5718E
DyLight 488	FAB5718K
DyLight 550	FAB5718L
DyLight 594	FAB5718M
DyLight 650	FAB5718W
DyLight 680	FAB5718Y
DyLight 755	FAB5718Z
FITC	FAB5718F
HRP	FAB5718H
Janelia Fluor 525	FAB5718JF525
Janelia Fluor 549	FAB5718I
Janelia Fluor 646	FAB5718J
Janelia Fluor 669	FAB5718JF669
PE	FAB5718P
PerCP	FAB5718C
mFluor Violet 450 SE	FAB5718MFV450
mFluor Violet 500 SE	FAB5718MFV500
mFluor Violet 610 SE	FAB5718MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
Carrier Free	MAB5718-SP

compare

(select up to 3 products from this page to compare)

NBP1-47339

GAPDH Antibody (1A10) - BSA Free

(2 Reviews)

(12 Publications)

0.1 ml

NBP1-47339

Flow Cytometry: GAPDH Antibody (1A10) [NBP1-47339] - An intracellular stain was performed on U-87 cells with GAPDH [1A10] Antibody NBP1-47339AF488 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 488.

Immunocytochemistry/Immunofluorescence: GAPDH Antibody (1A10) [NBP1-47339] - GAPDH was detected in immersion fixed HeLa human cervical epithelial carcinoma cell line using 2 ug/mL of mouse anti-GAPDH monoclonal (NB300-328), 2 ug/mL mL of mouse anti- GAPDH monoclonal (NBP1-47339). Cells were stained using the appropriate secondary antibody donkey anti-mouse IgG-NL557 (NL007) and counterstained with DAPI (blue).

Immunohistochemistry-Paraffin: GAPDH Antibody (1A10) [NBP1-47339] - Analysis of paraffin-embedded human breast carcinoma (left) and kidney carcinoma (right), showing cytoplasmic localization using anti-GAPDH mAb with DAB staining.

Simple Western: GAPDH Antibody (1A10) [NBP1-47339] - Lane view shows a specific band for GAPDH in 1.0 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system. Note: band observed higher than predicted 36 kDa molecular weight.

Basal tissue factor (TF) and androgen receptor (AR) mRNA expression in prostate cancer cell lines. (A) Basal TF mRNA expression levels in DU145, PC3 and LNCaP cells as determined by quantitative PCR (qPCR) (n = 6). (B) Basal AR mRNA expression levels in DU145, PC3 and LNCaP cells as determined by qPCR (n = 6). (C) Correlation analysis of basal TF mRNA expression levels with basal mRNA expression levels of AR, specificity protein 1 (SP1), early growth response protein 1 (EGR1), p65, c‐Rel, I kappa B alpha , Jun and cFos mRNA (n = 6). (D) Western blot analysis of AR, TF, I kappa B alpha , p65, p50, c‐Rel, EGR1, SP1 and glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH) protein expression in DU145, PC3 and LNCaP cells. Error bars represent standard error of the mean. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/29427323), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu(-), Rt(-)

Species Glossary

Reactivity: Hu, Mu(-), Rt(-)

Applications:

, , , , ,

Applications: , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NBP1-47339AF350
Alexa Fluor 405	NBP1-47339AF405
Alexa Fluor 488	NBP1-47339AF488
Alexa Fluor 532	NBP1-47339AF532
Alexa Fluor 594	NBP1-47339AF594
Alexa Fluor 647	NBP1-47339AF647
Alexa Fluor 700	NBP1-47339AF700
Alexa Fluor 750	NBP1-47339AF750
Alexa Fluor Plus 405	NBP1-47339AFP405
Alexa Fluor Plus 488	NBP1-47339AFP488
Alexa Fluor Plus 555	NBP1-47339AFP555
Alexa Fluor Plus 594	NBP1-47339AFP594
Alexa Fluor Plus 647	NBP1-47339AFP647
Alexa Fluor Plus 680	NBP1-47339AFP680
Allophycocyanin	NBP1-47339APC
Biotin	NBP1-47339B
CoraFluor 1	NBP1-47339CL1
DyLight 350	NBP1-47339UV
DyLight 405	NBP1-47339V
DyLight 488	NBP1-47339G
DyLight 550	NBP1-47339R
DyLight 594	NBP1-47339DL594
DyLight 650	NBP1-47339C
DyLight 680	NBP1-47339FR
DyLight 755	NBP1-47339IR
FITC	NBP1-47339F
HRP	NBP1-47339H
Janelia Fluor 525	NBP1-47339JF525
Janelia Fluor 549	NBP1-47339JF549
Janelia Fluor 646	NBP1-47339JF646
Janelia Fluor 669	NBP1-47339JF669
PE	NBP1-47339PE
PerCP	NBP1-47339PCP
mFluor Violet 450 SE	NBP1-47339MFV450
mFluor Violet 500 SE	NBP1-47339MFV500
mFluor Violet 610 SE	NBP1-47339MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NBP1-47339SS
Azide and BSA Free	NBP2-80748

compare

(select up to 3 products from this page to compare)

NB300-325

GAPDH Antibody

(2 Reviews)

(4 Publications)

0.1 ml

NB300-325

Western Blot: GAPDH Antibody [NB300-325] - Whole cell lysate (50 ug) from HeLa (H) and 293T (50 ug) probed with GAPDH Antibody diluted at 0.04 ug/ml

Western Blot: GAPDH Antibody [NB300-325] - Detection of Mouse GAPDH Whole cell lysate (5, 15 and 50 ug) from mouse NIH3T3 cells. Another Affinity purified rabbit anti-GAPDH used at 0.04 mcg/ml. Chemiluminescence with an exposure time of 30 seconds.

Simple Western: GAPDH Antibody [NB300-325] - Simple Western lane view shows a specific band for GAPDH in 0.05 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.

Western Blot: GAPDH Antibody [NB300-325] - GCNY-medicated serum decreased Nrf2 levels & inflammatory cytokines of NF-kappa B & IL-6. (A) Intracellular relative ROS levels in HMC-3 cells treated with different concentrations (0, 50, 100, & 200 μm) of H2O2 for 4 h. Auto-fluo refers to the auto-fluorescence intensity value of HMC-3 cells. (B,C) The mRNA & protein levels of Nrf2 were expressed by HMC-3 treated with different concentrations of H2O2. (D) The significantly elevated whole protein level in NC + H2O2 group cells indicates an increased proliferation of HMC-3 cells compared to the NC group cells & (E) ROS levels were attenuated in cells treated by GCNY-medicated serum. (F–H) Through automated Western blot analysis, GCNY group cells expressed lower levels of Nrf2, NF-kappa s p65, pNF-kappa B p65 (ser536), & IL-6 compared with NC + H2O2 group cells. ns, no significance, *p < 0.05; **p < 0.01; ***p < 0.001; ****p < 0.0001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/36188472), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt

Species Glossary

Reactivity: Hu, Mu, Rt

Applications:

, , ,

Applications: , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Conjugate:

Unconjugated

compare

(select up to 3 products from this page to compare)

At	=	A. thaliana	SyHa	=	Golden Syrian Hamster
All	=	All Species	Ha	=	Hamster
An	=	Animal	Hu	=	Human
ArHa	=	Armenian Hamster	I	=	Insect
Av	=	Avian	Ll	=	Llama
Bb	=	Baboon	Ma	=	Mammal
Ba	=	Bacteria	Mk	=	Monkey
Bv	=	Bovine	Mu	=	Mouse
Ca	=	Canine	Multi	=	Multi-species
Ce	=	C. Elegans	NA	=	Non-species specific
Ch	=	Chicken	Or	=	Orangutan
ChHa	=	Chinese Hamster	Pl	=	Plant
Cm	=	Cynomolgus Monkey	Pm	=	Primate
Do	=	Donkey	Po	=	Porcine
Dr	=	Drosophilia	Rb	=	Rabbit
Ec	=	E. Coli	Rt	=	Rat
Eq	=	Equine	RM	=	Rhesus Macaque
Fe	=	Feline	Sh	=	Sheep
Ft	=	Ferret	Vb	=	Vertebrate
Fi	=	Fish	Vi	=	Virus
Fu	=	Fungi	Xp	=	Xenopus
Ge	=	Gerbil	Ye	=	Yeast
GP	=	Guinea Pig	Ze	=	Zebrafish
Gt	=	Goat

Category

Protein/Target

Applications

Reactivity

Citation

Antibody Validation

Reviews

Host

Available Conjugates

Format

Modification

Clonality

Clone

Images Type

Isotype

Preservative

Protein Or Peptide

Research Areas

Has Sample Size

Promotional Item

Species Glossary

Products Related to Gene-ID: 2597

GAPDH Antibody (1D4) - BSA Free

GAPDH Antibody - BSA Free

GAPDH Antibody [Unconjugated]

GAPDH Antibody (6C5cc) - BSA Free

GAPDH Antibody

GAPDH Antibody [Unconjugated]

GAPDH Antibody

GAPDH Antibody

GAPDH Antibody (13H12) - BSA Free

GAPDH Antibody (686613) [Unconjugated]

GAPDH Antibody (1A10) - BSA Free

GAPDH Antibody