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NB300-221

GAPDH Antibody (1D4)

(19 Reviews)

(411 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.

Application of the approach to other cell lines. The remainder of the protocol from Figure 2 was then applied using 100 ug/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 and probing with antibodies to GAPDH, BiP and Histone H3 (Used as an alternative nuclear marker due to weakness of the Lamin A signal in HeLa cells). Image collected and cropped by CiteAb from the following publication (//bmcresnotes.biomedcentral.com/articles/10.1186/1756-0500-2-243) licensed under a CC-BY license.

Endothelial responses provoked by Hb-lipid interactions are attenuated by sulfide donors. Confluence HAoECs were exposed to the obtained Hb samples for 8 hours and VCAM-1 expression was determined by Western blotting. GAPDH were used as a loading control. Representative experiment, n = 3. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/omcl/2018/3812568/), licensed under a CC-BY license.

Regulation of cell migration-associated proteins by NCKU-21 in A549 and CL1-5 cells. Protein expressions of matrix metalloproteinase-2 (MMP-2) and MMP-9 were analyzed in A549 cell treated with NCKU-21 for 24 hr. * P 80% of endogenous Sin1 while levels of myc-FL Sin1 associated with Rictor are comparable with endogenous Sin1 levels. Image collected and cropped by CiteAb from the following open publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.20086), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunodepletions and the effects of RNases and various transcription inhibitors on chromosome condensation and cell cycle state.(A) Western blot for CAP-E, XPB, and Tubulin in Mock or CAP-E depleted extracts. Dilution series of Mock-depleted extracts was used to calculate the % depletion of CAP-E using quantitative fluorescence. (B) 1% agarose gel stained with SYBR safe stain showing RNase A dependent removal of total RNAs from high-speed supernatant egg extracts. (C) Representative fluorescence images of chromatid assembly at steady state (180 min after sperm addition) in the presence of indicated buffers and enzymes. See Materials and methods for details. Note that the high salt in the RNase H buffer causes morphological changes to chromatids regardless of activity. Mean condensation parameters for each condition are indicated in lower left corner of each image. (D) Western blot for XPB and Tubulin in IgG or XPB-depleted extracts. Dilution series of IgG-depleted extracts was used to calculate the % depletion of XPB using quantitative fluorescence. (E) Western blot for XPF, ERCC1, and Tubulin in IgG or ERCC1-depleted extracts. Dilution series of IgG-depleted extracts was used to calculate the % depletion of ERCC1 and XPF using quantitative fluorescence. (F) Representative fluorescence images of chromatid assembly at steady state (180 min after sperm addition) in the presence of DMSO, 30 μM CDK7 inhibitor THZ1, or 30 μM THZ1 and 50 μM triptolide (TPL). (G) Triptolide does not affect CDK1 activation or maintenance of M phase. Western blot for CDK1 T161ph, histone H3T3ph, and Tubulin in M phase HSS extracts in the presence of DMSO or 50 μM triptolide. Both CDK1T161ph (a CDK7 substrate) and H3T3ph are only highly phosphorylated in M phase, and their appearance is not affected by triptolide treatment.Figure 1—figure supplement 1—source data 1.Source data for Figure 1—figure supplement 1A, B,D, E, G.Source data for Figure 1—figure supplement 1A, B,D, E, G. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35293859), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Activation of the ATM‐Chk2‐p53 pathway upon CDDP treatmentAConfocal images showing the basal region of organ of Corti cultures treated with either culture medium alone or medium containing 10 μM CDDP for 1 day and immunolabeled for myosin 7A (red) and p‐ATM (green). Scale bar = 15 μm.BHigher magnification images showing representative OHC and IHC nuclei from control and CDDP‐exposed cells. Scale bar = 5 μm.CHistograms displaying green fluorescent signal intensity of x‐projections of OHC and IHC nuclei from control and CDDP‐exposed cells.DQuantification analysis of p‐ATM foci numbers in both OHCs and IHCs exposed to either culture medium alone (light blue and red lines for OHCs and IHCs, respectively) or 10 μM CDDP (blue and red lines for OHCs and IHCs, respectively; n = 50 nuclei per condition and per time point). Data are expressed as mean ± SEM. One‐way ANOVA test followed by post hoc Tukey's test (**P < 0.008, ***P = 0.00005; CDDP‐exposed OHCs versus CDDP‐exposed IHCs).EHigher magnification confocal and 3D images showing the co‐localization of p‐ATM foci (green) with 53BP1 foci (red) in an OHC nucleus from the basal region of the organ of Corti culture treated with 10 μM CDDP for 1 day. Scale bar = 5 μm.FConfocal images showing the basal region of organ of Corti cultures treated with either culture medium alone or medium containing 10 μM CDDP for 1 day and immunolabeled for myosin 7A (red) and p‐Chk2 (green). Scale bar = 15 μm.GHistograms of green fluorescent signal intensity from OHC and IHC nuclei of a CDDP‐treated organ of Corti explant.HQuantification of Chk2‐positive nuclei in both IHCs (red bars) and OHCs (blue bars) from control and CDDP‐treated organ of Corti cultures (n = 50 nuclei per condition and per time point). Data are expressed as mean ± SEM. Kruskal–Wallis test followed by post hoc Dunn's test (*P = 0.045, ***P = 0.0002; CDDP‐exposed IHCs versus control IHCs, CDDP‐exposed OHCs versus control OHCs).IRepresentative Western blots using antibodies against p‐p53 (serine 15), p53, and beta ‐actin in control and 10 μM CDDP‐exposed whole cochlear extracts.J, KHistograms representing the levels of total p53 protein (J) and p53 phosphorylation (K) in control (gray bars) and CDDP‐exposed cochleae (green bars; n = 6 cochleae per condition and per time point). Actin served as a loading control. Data are expressed as mean ± SEM. One‐way ANOVA test followed by post hoc Tukey's test (J: *P ≤ 0.023; K: *P = 0.032, **P = 0.007, ***P ≤ 0.0008; cochleae at the different times after CDDP exposure versus control 12 h).Data information: All experiments were performed in triplicate. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27794029), 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

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NBP2-27103

GAPDH Antibody (13H12) - BSA Free

(3 Reviews)

(32 Publications)

0.1 mg

NBP2-27103

Immunocytochemistry/Immunofluorescence: GAPDH Antibody (13H12) [NBP2-27103] - GAPDH antibody was tested in HeLa cells with Dylight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and Dylight 550 (red). A dilution of 1:10 was used. Image objective 40x.

Western Blot: GAPDH Antibody (13H12) [NBP2-27103] - WB detection of GAPDH protein (theoretical molecular weight: 36 kDa) in HeLa cells lysate using GAPDH antibody (clone 13H12) in (A) the absence and (B) the presence of immunizing peptide.

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.

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

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

Western Blot: GAPDH Antibody (13H12) [NBP2-27103] - Serum from trauma patients induces intrinsic apoptosis resistance by up-regulating AAT expression in neutrophils. AAT protein expression was analyzed in neutrophils after 18 h of culture by western blot analysis. Relative expression was quantified vs. GAPDH expression. One representative blot of five independent experiments is depicted. **p<0.01 (one-way ANOVA with Newman keuls post-hoc test). Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0177450), licensed under a CC-BY license.

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 section of normal human stomach tissue using GAPDH antibody (clone 13H12) at 5 ug/ml concentration.

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

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.

5-FU-produced ROS involved in histone methyltransferase-mediated Nrf2 expressionSNUC5/5-FUR cells were pre-treated with 500 μM NAC, plated, and incubated for 48 h. Then, cells were treated with 10 μM DHR123 and incubated for 30 min at 37°C. The intracellular ROS were detected by A. flow cytometry and B. confocal imaging. FI indicates the fluorescence intensity of DHR-123. *Significantly different from SNUC5 cells (p<0.05), and #significantly different from SNUC5/5-FUR cells (p<0.05). C. Expression pattern of Nrf2 mRNA was determined by RT-PCR analysis. *Significantly different from SNUC5 cells (p<0.05), and #significantly different from SNUC5/5-FUR cells (p<0.05). D. Expression pattern of nuclear and cytosolic Nrf2 protein was determined by Western analysis. E. Expression patterns of TET1, OGT, HCF1, and MLL in NAC pre-treated SNUC5/5-FUR cells determined by Western blot analysis. *Significantly different from SNUC5 cells (p<0.05), and #significantly different from SNUC5/5-FUR cells (p<0.05). Also, SNUC5 cells were pre-treated with 500 μM of NAC and incubated for an additional 1 h at 37°. Cells were then treated with 140 μM 5-FU for 48 h. 10 μM of DHR123 was added to plate and incubated for an additional 30 min at 37°C. F. The intracellular ROS level was detected by flow cytometry and G. confocal imaging. FI indicates the fluorescence intensity of DHR123. *Significantly different from SNUC5 cells (p<0.05), and #significantly different from 5-FU-treated SNUC5 cells (p<0.05). H. Expression pattern of Nrf2 mRNA was determined by RT-PCR analysis. *Significantly different from SNUC5 cells (p<0.05), and #significantly different from 5-FU-treated SNUC5 cells (p<0.05). I. Expression pattern of nuclear and cytosolic Nrf2 protein was determined by Western analysis. J. The expression of TET1 and interaction proteins detected by Western blot analysis. *Significantly different from SNUC5 cells (p<0.05), and #significantly different from 5-FU-treated SNUC5 cells (p<0.05). Image collected and cropped by CiteAb from the following open publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.9745), 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:

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
Biotin	NBP2-27103B
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 549	NBP2-27103JF549
Janelia Fluor 646	NBP2-27103JF646
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

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NB300-327

GAPDH Antibody

(3 Reviews)

(45 Publications)

0.1 ml

NB300-327

Western Blot: GAPDH Antibody [NB300-327] - 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. Image collected and cropped by CiteAb from the following publication (//nanoscalereslett.springeropen.com/articles/10.1186/1556-276X-8-195), licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: GAPDH Antibody [NB300-327] - Analysis of HeLa cells stained with rabbit pAb to GAPDH, dilution 1:2000 in red. Blue is Hoescht staining of nuclear DNA. The GAPDH antibody produces diffuse cytoplasmic staining of cells.

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.

$Western Blot: GAPDH Antibody [NB300-327] - Effects of subchronic administration (7 and 14 days) of therapeutic relevant concentration of Brex (Brex: 300 nM) and interaction between Brex and 5-HT1A receptor (5-HT1AR) antagonist WAY (10 uM) on protein expression of 5-HT1A receptor in the plasma membrane fraction of cortical primary cultured astrocytes. In left side histograms, ordinate: mean +/- SD (n = 6) of the relative protein level of 5-HT1AR per GAPDH. * p < 0.05, ** p < 0.01: relative to control (Brex-free) by one-way analysis of variance (ANOVA) with Tukey’s post-hoc test, and @ p < 0.05: relative to Brex for 14 days by Student’s T-test. Right side panels indicate their pseudo-gel images using capillary immunoblotting. Antibodies used: 5-HT1A (NBP2-21590) and GAPDH (NB300-327). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35743014/) licensed under a CC-BY license.$

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.

Growth of lactobacilli on IECs and their influence towards C. albicans cytotoxicity, adhesion, hyphal length and translocation. (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) and infected with C. albicans for 6, 12 and 24 h. Data are mean+/-s.e.m. *P<0.05, **P<0.01, ***P<0.005 (t-test). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31413153), licensed under a CC-BY licence.

HMGB1 regulated autophagy in thyroid cancer cells (a) FTC-133/TPC-1 cells were transfected with HMGB1 shRNA and control shRNA and then starved by HBSS for 2 h. And LC3-I/II level was assayed by Western blot; (b) FTC-133/TPC-1 cells were transfected with HMGB1 shRNA and control shRNA and then pre-treated for 1 h with pepstatin A (PA, 10 μM) and E64D (10 μM) as indicated. Cells were subsequently treated for 3 h with HBSS in continuous presence or absence PA/E64D inhibitors. LC3-I/II, Beclin1 and p62 levels were assayed by Western blot; (c) Ultrastructural features in FTC-133/TPC-1 cells transfected with HMGB1 shRNA and control shRNA after a 3-h treatment of HBSS. More autophagosomes were seen in control shRNA plus HBSS-treated cells than in cells treated with HMGB1 shRNA plus HBSS. Arrows indicated autophagosomes Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31331356), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Compound MI-743 causes intracellular 8-oxo-dG accumulation and DNA damage.a MGC-803, HGC-27 and GES-1 cells were treated with DMSO or 5 µM MI-743 for 48 h. Intracellular 8-oxo-dG was stained with Cy3-conjugated avidin. DNA was counterstained with 4,6-diamidino-2-phenylindole (DAPI). Images were acquired at ×100 magnification by a Nikon Eclipse TE 2000-S fluorescence microscope. At least three independent experiments were performed for each group. b MGC-803, HGC-27 and GES-1 cells were treated with DMSO or 10 µM MI-743 for 48 h and run in alkaline comet assay. Pictures were originally captured at ×40 magnification. H2O2 was used as positive control. c Tail moment was calculated by CometScore software. Three individual experiments were performed for each group. d–f Western blot analysis of the protein levels of MTH1, MUTYH, OGG1, p21, ATMpS1981 and p53pS15 in MGC-803, HGC-27 and GES-1 cells, treated with increasing concentrations of MI-743 (0, 1, 2, 4, 8 and 12 µM). g, h Densitometry shows relative protein expression normalized for GAPDH. Data are representative of three independent experiments. i–k Western Blot analysis of the protein levels of MTH1, MUTYH, OGG1, p21, ATMpS1981 and p53pS15 of protein lysates, isolated from MGC-803, HGC-27 and GES-1 cells, which were treated with 12 µM MI-743 for 0, 12, 24, 36 and 48 h. l, m Densitometry shows relative protein expression normalized for GAPDH. Data are presented as means ± SD. Three individual experiments were performed for each group. *P < 0.05, **P < 0.01, ***P < 0.001 as compared with the controls Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31164636), 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

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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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