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NB600-502

GAPDH Antibody (6C5cc)

(3 Reviews)

(81 Publications)

0.2 mg

NB600-502

Western Blot: GAPDH Antibody (6C5) [NB600-502] - MUS81 promotes DNA synthesis during mitosis in BRCA2-deficient cells. Cell extracts were immunoblotted as indicated. SMC1 and GAPDH were used as loading controls. Image collected and cropped by CiteAb from the following publication (//www.nature.com/doifinder/10.1038/ncomms15983), licensed under a CC-BY license.

Western Blot: GAPDH Antibody (6C5) [NB600-502] - Western blot analysis of GAPDH expression in 1) HeLa, 2) NTERA-2, 3) A-431, 4) HepG2, 5) MCF-7, 6) NIH 3T3, 7) PC-12 and 8) COS-7 whole cell lysates. Theoretical molecular weight: 36 kDa.

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.

Representative picture of western blot in histopathologically unchanged tissue (N) and primary cancerous tissue (C) from patients with CRC. Immunodetection of bands was performed with Rp anti- PHD1, - PHD2, - PHD3 and - FIH Ab, followed by incubation with goat anti-rabbit HRP-conjugated Ab. The membrane was stripped and incubated with Rp anti-GAPDH Ab, followed by incubation with goat anti-rabbit HRP-conjugated Ab. Bands were revealed using SuperSignal West Femto Chemiluminescent Substrate, Thermo Fisher Scientific (Rockford, IL) and Biospectrum® Imaging System 500, UVP Ltd. (Upland, CA). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/24195777), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunostaining of HN30 and MCF-12a cells for TRAF2 3 days post-transfectionMCF-12a NT (DAPI): non-treated MCF-12a DAPI stained, MCF-12a NT (TRAF2-FITC): non-treated MCF-12a FITC stained for TRAF2, MCF-12a pNSP 5a3a (DAPI): MCF-12a transfected with pcDNA 3.0 NSP 5a3a DAPI stained, MCF-12a pNSP 5a3a (TRAF2-FITC): MCF-12a transfected with pcDNA 3.0 NSP 5a3a FITC stained for Traf-2, HN30 NT (DAPI): non-treated HN30 DAPI stained, HN30 NT (TRAF2-FITC): non-treated HN30 FITC stained for TRAF2, HN30 pNSP 5a3a (DAPI): HN30 transfected with pcDNA 3.0 NSP 5a3a DAPI stained, HN30 pNSP 5a3a (TRAF2-FITC): HN30 transfected with pcDNA 3.0 NSP 5a3a FITC stained for TRAF2. White arrows indicate apoptotic bodies. Image collected and cropped by CiteAb from the following open publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.306), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Baclofen reversed the changes of protein markers characteristic for autophagy in hippocampal CA1 area under chronic cerebral hypoperfusion.(a–c) Five weeks after induction of hypoperfusion, p-mTOR was significantly decreased, and LC3-II, Beclin 1, atg5 and atg7 were significantly increased, and baclofen could reverse the changes of these proteins expression. Treatment with baclofen at 12.5 mg/kg and 25 mg/kg in sham-operated rats did not change the expression of LC3-II, mTOR, p-mTOR, Beclin 1, atg5 and atg7 compared with sham-operated rats (n = 4 in each group). Blots shown have been cropped to fit space requirements and run under the same experimental conditions. *P < 0.05 and **P < 0.01 vs sham-operated rats; ##P < 0.01 vs 2VO rats. Image collected and cropped by CiteAb from the following open publication (//www.nature.com/articles/srep14474), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

The production of DSBs depends on Top1 degradation in CPT-treated quiescent cells. (A–C) Serum-starved WI38 hTERT cells were co-transfected with siRNAs against cullin 3 and cullin 4B or against a control sequence and then treated with DMSO (−CPT) or 25 μM CPT (+CPT) for 1 h. (A and B) Western blotting of the indicated proteins. alpha Tubulin: loading control. (C) Number of gamma H2AX foci per nucleus from one representative experiment (246–348 nuclei were analyzed for each treatment) out of three. ***P < 0.001. (D and E) Serum-starved WI38 hTERT cells were treated with DMSO or MG132 (50 μM) for 1 h before exposure to 0.8 Gy IR. One hour post-irradiation, cells were co-stained for gamma H2AX (green) and 53BP1 (red). (D) Representative pictures. (E) Number of gamma H2AX foci per nucleus from one representative experiment (162–180 nuclei were analyzed for each treatment) out of three. Ns: not significant. (F and G) U2OS EV28 cells were treated with DMSO or MG132 (10 μM) for 1 h before the addition of ethanol (untreated) or 300 nM 4-hydroxitamoxifen (4OHT) for 4 h to express AsiSI in the nucleus (42). (F) Representative pictures of cells co-stained for gamma H2AX (green) and 53BP1 (red). (G) ChIP analysis using an anti-gamma H2AX antibody (black) or a non-immune antibody (IgG, gray). Enrichment was assessed by QPCR amplification using primers proximal to two AsiSI sites located inside two genes (Gene I: SFRS6, Gene II: CCD47) and primers distal to an AsiSI site (Control). Enrichment was normalized to the maximum recovery for each experiment (means ± SEM, n = 3). Ns: not significant; *P < 0.05. In the microscopic images, nuclear contours, identified by DAPI staining (not shown), are indicated by dashed lines. Bars: 10 μm. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/26578593), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

GFAP expression and synthesis in the ON and ONH in a murine glaucoma model. (A) GFAP immunoreactivity in the glial lamina of 1-month (green, upper panel) and 2 months (green, middle and lower panel) old beta B1-CTGF1 mice compared to WT controls. Immunoreactivity of GFAP was not altered in 1-month old TG and WT animals (green, upper panel). 2 month old beta B1-CTGF1 mice showed an increased GFAP immunoreactivity compared to WT control (green, middle panel). Lower panel shows a magnified detail of the middle panel. Nuclei are stained with Dapi (blue). (B) Schmatic illustration of the optic nerve. A depicts the region in the glial lamina where cross sections were obtained. ONH (unmyelinated part) and ON (myelinated part) were used for molecular analysis. (C) Quantification of immunohistochemical staining of GFAP in the glial lamina is not altered in 1 month old TG and WT animals (WT: n = 5; TG: n = 4). GFAP immunoreactivity is increased in 2 month old TG animals compared to WT littermates (WT: n = 10, TG: n = 13; *p = 0.039; two-tailed t-test compared to theoretical mean of 1 (normalized control)). Mean value of WT animals (control) was set at 1. (D) RT-PCR analyses revealed no alteration in the Gfap mRNA expression in the ON of 1-month (WT: n = 7; TG: n = 5) and 2 month old beta B1-CTGF1 mice (WT: n = 15; TG: n = 16) compared to WT controls. In the ONH the Gfap mRNA expression is increased in the 2 month old TG compared to WT animals (WT: n = 6, TG: n = 5; *p = 0.04). The mRNA expression of Gfap is not altered in 1 month old animals (WT: n = 6, TG: n = 5). Mean value of WT animals (control) was set at 1. RPL32 was used to normalize mRNA expression. Data represented as mean ± SEM. PRL, Prelaminar region; PSL, Postlaminar region; ON, optic nerve; ONH, optic nerve head. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35493079), 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
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 549	NB600-502JF549-0.2ml
Janelia Fluor 646	NB600-502JF646-0.2ml

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NB300-322

GAPDH Antibody

(2 Reviews)

(39 Publications)

0.1 ml

NB300-322

Simple Western: GAPDH Antibody [NB300-322] - Simple Western 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 molecular weight of 36 kDa.

Western Blot: GAPDH Antibody [NB300-322] - Detection of Human and Mouse GAPDH (theoretical molecular weight: 36 kDa) by Western Blot. Samples: Whole cell lysate (15 ug) from HeLa, 293T, Jurkat, mouse TCMK-1, and mouse NIH3T3 cells prepared using NETN lysis buffer. Antibody: Affinity purified rabbit anti-GAPDH antibody NB300-322 used for WB at 0.1 ug/ml. Detection: Chemiluminescence with an exposure time of 30 seconds.

Western Blot: GAPDH Antibody [NB300-322] - Detection of Human and Mouse GAPDH (theoretical molecular weight: 36 kDa) by Western Blot. Samples: Whole cell lysate from mouse NIH3T3 (5, 15 and 50 ug) and human HeLa (H; 50 ug) cells. Antibody: Affinity purified rabbit anti-GAPDH antibody used at 0.04 ug/ml. Detection: Chemiluminescence with an exposure time of 30 seconds.

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

Western Blot: GAPDH Antibody [NB300-322] - c-Src is required for efficient translation of PRC2 component mRNAs. Immunoblot of PRC2 components in control and c-Src-deficient tumors. Bar chart shows quantification of fluorescent immunoblot data normalized to the loading control (Gapdh). Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-019-10681-4), licensed under a CC-BY license.

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.

Western Blot: GAPDH Antibody [NB300-322] - Gem expression is sufficient to increase chemokinesis and chemotaxis. Western blot analyses were performed on 70 ug 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 and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.ppat.1003917) licensed under a CC-BY license

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.

$Effects of subchronic nicotine administration on the expression of phosphorylated protein kinase B (pAkt) and phosphorylated extracellular signal-regulated kinase (pErk) in the plasma membrane fraction of OFC. Effects of the systemic subchronic administration of nicotine (50 mg/kg/day for seven days) on pAkt and pErk expression in the OFC plasma membrane fraction before four week of age (A,C) and after 12 week of age (B,D), ADSHE onset of the wild-type and S286L-TG and pseudo-gel images, using capillary immunoblotting. Ordinate: mean +/- SD (n = 6) of the relative protein level of pErk and pAkt. * p < 0.05, ** p < 0.01 vs. wild-type, and @ p < 0.05, @@ p < 0.01 vs. nicotine-free (non) by two-way ANOVA with Tukey's multiple comparison. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33143372), licensed under a CC-BY licence.$

$Concentration-dependent effects of the subchronic administration of LCM (30 or 100 uM), CBZ (30 or 100 uM), and ZNS (30, 100, or 300 uM) on the Cx43 expression in the plasma membrane fraction of primary cultured astrocytes (A) and pseudo-gel images using the Simple Western results with anti-Cx43 (B) and anti-GAPDH (C) antibodies for blotting of the plasma membrane fractions. In (A), ordinate: mean +/- SD (n = 6) of the relative protein level of Cx43. * p < 0.05 relative to the control by one-way ANOVA with Tukey's multiple comparison. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32516974), licensed under a CC-BY licence.$

c-Src is required for efficient translation of PRC2 component mRNAs. A) Immunoblot of PRC2 components in control and c-Src-deficient tumors. Bar chart shows quantification of fluorescent immunoblot data normalized to the loading control (Gapdh). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31263101), licensed under a CC-BY licence.

Silencing NUSAP1 inhibits cell proliferation and causes apoptosis in GBM cells. a Western blot analyses of NUSAP1 in cells with NUSAP1 knockdown. b The morphology and cell number of GBM cells after knocking down NUSAP1. c Viability of NUSAP1-knockdown GBM cells. d BrdU-positive GBM cells after knocking down NUSAP1. e Flow cytometry analyses of apoptosis in GBM cells with NUSAP1 knockdown. f The expression of the apoptotic proteins bcl2 and cleaved caspase-3 in cells with NUSAP1 knockdown. g Caspase-3/7 activity of GBM cells with NUSAP1 knockdown. All data are expressed as the mean ± SD, and significant differences were determined by Student’s t test. *P < 0.05, **P < 0.01, ***P < 0.001. P < 0.05 was considered statistically significant Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/32317623), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Effects of anti-S100a9 Ab on the frequency of neutrophils, macrophages, and dendritic cells (DCs) in the colon of the dextran sulfate sodium (DSS) mouse model. (A) Colon lamina propria cells were isolated from normal control and IgG Ab or anti-S100a9 Ab-treated DSS mice at day 6 post-DSS colitis induction. Frequencies of neutrophils, macrophages, and DCs in the colon were determined by flow cytometry. Cells were gated on CD45+CD3−CD4−CD11b+Ly6G+, CD45+CD3−CD4−CD11b+F4/80+, and CD45+CD3−CD4−CD11b+CD11c+ populations respectively. Representative flow cytometric figures were shown. The percentage of cells was presented as the mean ± SEM of four to six individual mice per group. *p < 0.05 in a one-way analysis of variance followed by Bonferroni correction. Data were representative of three independent experiments. (B) Immunohistochemical staining of myeloperoxidase (MPO), CD68, and CD11c proteins in the normal control and IgG Ab or anti-S100a9 Ab-treated colitis mice at day 6 (left panels: original magnification 40×, scale bar: 200 µm; right panels: original magnification 200×, scale bar: 50 µm). Staining scores were counted. One-way analysis of variance followed by Bonferroni correction. Results were representative of the three experiments performed. Error bars represent SD. (C) Expression of S100a9, Tnf alpha , Il1 beta , Il6, Il17a, Ifn gamma , Il12a, Il23a, Il4, and Il10 mRNA, as assessed by quantitative real-time PCR in normal control and IgG Ab, or anti-S100a9 Ab-treated colitis tissues. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/29326691), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

[18F]PBR06 selectivity in primary human grade IV glioblastoma xenotransplant.(A) Dynamic PET image (axial) pre-infusion of cold analog, with [18F]PBR06 uptake primarily confined to the tumor. (B) Dynamic PET image (axial) post-infusion, showing nearly total displacement of [18F]PBR06. (C) Time-activity curves of injected [18F]PBR06 in tumor (green) and contralateral brain (blue). (D) Correlative TSPO immunohistochemistry, Tumor + White Matter Tract (40X). Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0141659), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Analysis of the expression of the transgene in C-IKK alpha and N-IKK alpha tumors by biochemical and immunohistochemical approachesA. Western blot showing the increased expression of IKK alpha in transgenic mice. B-I. Immunohistochemistry showing the expression of the transgenic protein in N-IKK alpha and C-IKKa tumors. Staining with NB100-56704 antibody is shown. (B, C) Representative images showing the expression of transgenic IKK alpha in tumors and adjacent skin of N-IKK alpha /TgAC mice (B), and C-IKK alpha /TgAC animals (C). (D, E) Detail showing the nuclear (D) or cytoplasmic (E) localization of the transgenic IKK alpha in tumors. (F, G) Similar levels of expression of the transgenic IKK alpha in different N-IKK alpha tumors. By contrast variable levels of expression of the transgene are observed between different C-IKK alpha tumors (H, I). t: tumor; s: non-tumoral skin. Scale bar: (B, C) 100μm; (D, E) 80 μm; (F-I) 200 μm. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27121058), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Protein expressions of intrarenal RAS components in two groups of mice. (A) Immunohistochemical analysis of intrarenal RAS expression position in the two groups of mice. AGT immunoreactivity in the proximal tubular cells, Ang II immunoreactivity in both glomerular and tubular cells, renin immunoreactivity in juxtaglomerular apparatus cells, ACE immunoreactivity in brush border membranes of proximal tubules as well as AT1 and AT2 immunoreactivity in the proximal tubules were increased in the HF group when compared to the control group. (B) Western blot analysis for protein expressions of intrarenal RAS components in the two groups of mice. (C) The histogram represents mean ± SD of the densitometric scans for the protein bands of angiotensinogen (AGT), angiotensin II (Ang II), renin, angiotensin converting enzyme (ACE), angiotensin II type 1 receptor (AT1), angiotensin II type 2 receptor (AT2) from five experiments, normalized by beta -actin. * P < 0.05 vs. control. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/23570453), licensed under a CC-BY license. 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

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