Invitrogen

GAPDH Loading Control Monoclonal Antibody (GA1R), Alexa Fluor™ 647

13 Published Figures

View all (118) GAPDH antibodies

Questions & Answers

Questions & Answers

Antibody Testing Data (2)
Published Figures (13)

GAPDH Loading Control Antibody in Immunocytochemistry (ICC/IF)

GAPDH Loading Control Antibody in Immunocytochemistry (ICC/IF)

FIGURE: 1 / 15

GAPDH Loading Control Antibody (MA5-15738-A647) in ICC/IF

Immunofluorescent analysis of GAPDH (red) in HeLa cells. The cells were fixed with 4% paraformaldehyde for 15 minutes, permeabilized with 0.1% Triton X-100 in PBS for 15 minutes and blocked with 3% Blocker BSA (Product # 37525) in PBS for 30 minutes at room temperature. Cells were stained with AlexaFluor 647 conjugated GAPDH monoclonal antibody (Product # MA5-15738-A647) at a dilution of 1:50 for 1 hour at ... View More

GAPDH Loading Control Antibody in Immunocytochemistry (ICC/IF)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

GAPDH Loading Control Antibody in Western Blot (WB)

Product Image Gallery

GAPDH Loading Control Antibody in Immunocytochemistry (ICC/IF) — Immunofluorescent analysis of GAPDH (red) in HeLa cells. The cells were fixed with 4% paraformaldehyde for 15 minutes, permeabilized with 0.1% Triton X-100 in PBS for 15 minutes and blocked with 3% Blocker BSA (Product # 37525) in PBS for 30 minutes at room temperature. Cells were stained with AlexaFluor 647 conjugated GAPDH monoclonal antibody (Product # MA5-15738-A647) at a dilution of 1:50 for 1 hour at room temperature. Nuclei (blue) were stained with Hoechst 33342 dye (Product # 62249). Images were taken on a Thermo Scientific ToxInsight at 20X magnification.

GAPDH Loading Control Antibody in Western Blot (WB) — Western blot analysis of GAPDH was performed by loading various cell lysates onto a 4-20% Tris-HCl polyacrylamide gel. Proteins were transferred to a low fluorescence PVDF membrane and blocked with Sea Block blocking buffer for at least 1 hour. The membrane was probed with a AlexaFluor647-conjugated GAPDH monoclonal antibody (Product # MA5-15738-A647) at a dilution of 1:500 for over night at 4C on a rocking platform and washed in TBS-0.1% Tween-20. Detection was performed using a fluorescence imaging system.

GAPDH Loading Control Antibody in Western Blot (WB) — Published figure using GAPDH Loading Control monoclonal antibody (Product # MA5-15738-A647) in Western Blot

GAPDH Loading Control Antibody in Western Blot (WB) — Published figure using GAPDH Loading Control monoclonal antibody (Product # MA5-15738-A647) in Western Blot

GAPDH Loading Control Antibody in Western Blot (WB) — Published figure using GAPDH Loading Control monoclonal antibody (Product # MA5-15738-A647) in Western Blot

GAPDH Loading Control Antibody in Western Blot (WB) — Published figure using GAPDH Loading Control monoclonal antibody (Product # MA5-15738-A647) in Western Blot

GAPDH Loading Control Antibody in Western Blot (WB) — Figure 5. Western blotting analysis of Sw1353 cells at different time points following irradiation (X-rays and C-ions 28 keV/um). SW1353 cells were analyzed by Western blotting to estimate the variation kinetics of specific proteins markers to irradiation responses. A control (0 Gy) at 1 hour and irradiated samples (2 Gy) were compared from 1 to 96 hours following treatment. Different antibodies were used, gamma-H2AX, p21, and GAPDH were analyzed by Western blotting (A) and the corresponding signal was quantified with the Quantity One software (Bio-Rad, Hercules, California) and normalized against the signal of the GAPDH loading control (B). Gamma-H2AX and X-rays partially from Hamdi et al. 22 .

GAPDH Loading Control Antibody in Western Blot (WB) — Published figure using GAPDH Loading Control monoclonal antibody (Product # MA5-15738-A647) in Western Blot

GAPDH Loading Control Antibody in Western Blot (WB) — Published figure using GAPDH Loading Control monoclonal antibody (Product # MA5-15738-A647) in Western Blot

GAPDH Loading Control Antibody in Western Blot (WB) — Published figure using GAPDH Loading Control monoclonal antibody (Product # MA5-15738-A647) in Western Blot

GAPDH Loading Control Antibody in Western Blot (WB) — Figure 6 ATF6 is processed during L. pneumophila infection. ( a ) RAW 264.7 cells were left uninfected or infected with either WT L. pneumophila , DeltadotA , B. Delta5, Delta5+plgt2, or Delta5 plgt2* (catalytically dead lgt2) at an MOI of 150. Cells were then left untreated or treated with thapsigargin (Tg; 1 mug mul -1 ) for 6 h. Full-length ATF6 (pATF6) and cleaved pATF6(N) were monitored via immunoblot. Full blots for Fig. 6a are provided in Supplementary Fig. 5 . ( b ) HEK-293 FCgamma cells infected with either WT L. pneumophila or DeltadotA and then treated for 6 h with Tg (1 mug mul -1 ). Sel1L mRNA levels were then monitored via qRT-PCR, with GAPDH serving as an endogenous control. Two biological replicates were used each with three technical replicates using the identical experimental conditions. Values in all graphs are means+-s.e.m. * P <0.05; Student's t -test. ( c ) Cleaved and uncleaved ATF6 levels were similarly monitored in cells treated with CHX; 1 mug mul -1 ), Tg (1 mug mul -1 ), Tg and CHX, or left untreated for 6 h. Full blots for Fig. 6b are provided in Supplementary Fig. 5 . ( d ) RAW267.4 cells were infected with either WT L. pneumophila or the DeltadotA strain at an MOI of 150 and cells were then treated with Tg (1 mug mul -1 ) or left untreated for 6 h. ATF6 mRNA transcript levels were monitored via qRT-PCR. Two biological replicates were used each with three technical replicates using the identical experimental conditions. Values in all graphs

GAPDH Loading Control Antibody in Western Blot (WB) — Figure 3 Suppression of ER stress is an effector driven process that is independent of the mTOR pathway. ( a - c ) HEK-293 FCgamma cells were either left uninfected or infected with WT L. pneumophila or DeltadotA L. pneumophila at an MOI of 150. Cells were then either left untreated or treated with thapsigargin (Tg; 1 mug mul -1 ) or treated with a combination of Tg and the antibiotic Rifampicin (Rif.; 2 mug mul -1 ) for 6 h. After 6 h phase contrast images were taken. ( d ) HEK-293 FCgamma cells were infected at an MOI of 150 with WT L. pneumophila , or left uninfected. Cells were then treated with Rif. alone (2 mug mul -1 ), Rif. with Tg (1 mug mul -1 ), Tg (1 mug mul -1 ) alone or left untreated for 6 h. BiP protein levels were monitored via immunoblot. ( e ) HEK-293 FCgamma cells were untreated or treated with rapamycin (10 nM) or rapamycin with Tg (1 mug mul -1 ) for 6 h. BiP protein levels were then monitored via immunoblot and levels of phosphorylated Akt at serine 473 (P-Akt) were monitored from these lysates via immunoblot. ( f ) RAW 264.7 cells were infected with WT L. pneumophila, dotA , or Delta 5 strains of L. pneumophila at an MOI of 150. BiP protein expression was monitored via immunoblot. GAPDH was used as a loading control. Full blots for Fig. 3d-f are provided in Supplementary Fig. 5 .

GAPDH Loading Control Antibody in Western Blot (WB) — Figure 1 Expression of two critical components of the UPR, BiP and CHOP are blocked by L. pneumophila ( a ) Caspase 1/11 (-/-) bone marrow derived macrophages or ( b ) HEK-293 FCgamma cells-expressing Fc gamma (HEK-293 FCgamma) were either left uninfected or infected with WT or DeltadotA strains of L. pneumophila at an MOI of 150. Cells were then left untreated or treated with thapsigargin (Tg; 1 mug mul -1 ) for 6 h. BiP, CHOP and PDI protein expression were monitored via immunoblot. GAPDH was used as a loading control. Full blots are provided for Fig. 1a,b in Supplementary Fig. 5 . ( c , d ) BiP and CHOP levels were quantified respectively from three biological replicates using the same experimental conditions in HEK-293 FCgamma cells. Data are depicted as the fold change normalized to uninfected levels. Data represent three independent experiments. Values in all graphs are means+-s.e.m. * P <0.05; Student's t -test.

GAPDH Loading Control Antibody in Western Blot (WB) — Figure 6. The N-tails of H2A and H3 are epistatic to RAD18 . ( A ) Epistasis studies of (i) N-tail deletion mutants combinatorially deleted for (ii) MAG1 , (iii) REV3 , (iv) RAD5 and (v) RAD18 . ( B ) Epistasis study of N-tail deletion mutants combinatorially deleted for RAD52 . ( C ) MMS survival assay of WT and N-tail mutants (solid lines) and the N-tail mutants combinatorially deleted for RAD18 (dashed lines). ( D ) Growth curves of the cells in ( C ) in the absence of MMS. ( E ) Western blot of PCNA 9myc in WT and N-tail mutants before UV exposure and after a 1 h recovery in YPD following 100 J/m 2 of UV irradiation. GAPDH is used as the loading control. rad6Delta serves as a negative control for PCNA ubiquitylation. ( F ) Quantifications of (E) by normalizing (PCNA 9myc -ub)/(PCNA 9myc -total) and (PCNA 9myc -ub 2 )/(PCNA 9myc -total) to WT. Error bars indicate standard deviations from three independent experiments.

GAPDH Loading Control Antibody in Western Blot (WB) — Figure 3. Mag1 protein expression and MAG1 mRNA expression are reduced in tH2A:tH3 cells. WT and the N-tail deletion mutants were treated with 0.2% MMS for 10 min and further analyzed at the indicated time points. ( A ) Mag1 9myc and GAPDH were detected via western blotting. ( B ) A northern blot detecting MAG1 and reprobed for RDN18 . [We note that the small band shift between the tH3(60') sample and the tH2A:tH3 samples is due to a gel running artifact]. ( C ) Quantification of different gels, such as shown in (B) by normalizing MAG1 levels to that of WT in the absence of MMS. Error bars indicate standard deviations derived from three independent experiments.

Product Details

MA5-15738-A647

Applications

Tested Dilution

Publications

Western Blot (WB)

1:500

View 6 publications 6 publications

Immunocytochemistry (ICC/IF)

1:25-1:100

-

Product Specifications

Species Reactivity

Chicken, Hamster, Human, Insect, Mouse, Rabbit, Rat, Yeast, Bacteria

Published species

Human

Host/Isotype

Mouse / IgG1

Class

Monoclonal

Type

Antibody

Clone

GA1R

Immunogen

recombinant GAPDH

Conjugate

Alexa Fluor™ 647 Alexa Fluor™ 647 Alexa Fluor™ 647

Excitation/Emission Max

650/671 nm View spectra

Form

Liquid

Concentration

1 mg/mL

Purification

Protein A

Storage buffer

PBS with 1mg/mL BSA

Contains

0.05% sodium azide

Storage conditions

4°C, do not freeze

Shipping conditions

Ambient (domestic); Wet ice (international)

AB_2609745

Target Information

GAPDH (Glyceraldehyde-3-phosphate dehydrogenase) is a catalytic enzyme commonly known to be involved in glycolysis. GAPDH exists as a tetramer of identical 37-kDa subunits and catalyzes the reversible reduction of 1,3-bisphosphoglycerate to glyceraldehyde 3-phosphophate in the presence of NADPH. Apart from playing a key role in glycolysis, GAPDH is ubiquitously expressed and displays other activities unrelated to its glycolytic function. GAPDH is reported to be involved in the processes of DNA replication, DNA repair, nuclear RNA export, membrane fusion and microtubule bundling. Studies provide evidence of GAPDH playing an essential part in gene expression observed in apoptosis and as part of the cellular phenotype of age-related neurodegenerative diseases. Further, GAPDH is involved in other cellular processes ranging from membrane fusion, and neuronal apoptosis in cancer. GAPDH is reported to bind to a variety of other proteins, including the amyloid precursor protein, mutations in which cause some forms of Alzheimer's disease (AD), and the polyglutamine tracts of Huntingtin, the protein product aberrant forms of which are causative of Huntington's disease. Associations between GAPDH, actin and tubulin have also be reported. Since GAPDH is expressed at high levels in most tissues, it is useful as protein loading control in Western Blot analysis.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.

Product References

miR-29a Is Repressed by MYC in Pancreatic Cancer and Its Restoration Drives Tumor-Suppressive Effects via Downregulation of LOXL2.

Molecular cancer research : MCR

Dey S,Kwon JJ,Liu S,Hodge GA,Taleb S,Zimmers TA,Wan J,Kota J

Published figure using GAPDH Loading Control monoclonal antibody (Product # MA5-15738-A647) in Western Blot

Sat Feb 01 00:00:00 UTC 2020

High LET Radiation Overcomes In Vitro Resistance to X-Rays of Chondrosarcoma Cell Lines.

Technology in cancer research & treatment

Chevalier F,Hamdi DH,Lepleux C,Temelie M,Nicol A,Austry JB,Lesueur P,Vares G,Savu D,Nakajima T,Saintigny Y

Published figure using GAPDH Loading Control monoclonal antibody (Product # MA5-15738-A647) in Western Blot

Tue Jan 01 00:00:00 UTC 2019

Estradiol signaling mediates gender difference in visceral adiposity via autophagy.

Cell death & disease

Tao Z,Zheng LD,Smith C,Luo J,Robinson A,Almeida FA,Wang Z,Olumi AF,Liu D,Cheng Z

Published figure using GAPDH Loading Control monoclonal antibody (Product # MA5-15738-A647) in Western Blot

Thu Feb 22 00:00:00 UTC 2018

Protein-Protein Interactions Suggest Novel Activities of Human Cytomegalovirus Tegument Protein pUL103.

Journal of virology

Ortiz DA,Glassbrook JE,Pellett PE

Published figure using GAPDH Loading Control monoclonal antibody (Product # MA5-15738-A647) in Western Blot

Thu Sep 01 00:00:00 UTC 2016

The amino-terminal tails of histones H2A and H3 coordinate efficient base excision repair, DNA damage signaling and postreplication repair in Saccharomyces cerevisiae.

Nucleic acids research

Meas R,Smerdon MJ,Wyrick JJ

Published figure using GAPDH Loading Control monoclonal antibody (Product # MA5-15738-A647) in Western Blot

Tue May 26 00:00:00 UTC 2015

Legionella suppresses the host unfolded protein response via multiple mechanisms.

Nature communications

Treacy-Abarca S,Mukherjee S

Published figure using GAPDH Loading Control monoclonal antibody (Product # MA5-15738-A647) in Western Blot

Wed Jul 29 00:00:00 UTC 2015

Bioinformatics

Protein Aliases: 38 kDa BFA-dependent ADP-ribosylation substrate; aging-associated gene 9 protein; BARS-38; EC 1.2.1.12; epididymis secretory protein Li 278; epididymis secretory sperm binding protein Li 162eP; GAPDH; GAPDH-2; Glyceraldehyde-3-phosphate dehydrogenase; glyceraldehyde-3-phosphate dehydrogenase type 2; glyceraldehyde-3-phosphate dehydrogenase, spermatogenic; Glyceraldehyde-3-phosphate dehydrogenase, testis-specific; HGNC:4141; MGC88685; Peptidyl-cysteine S-nitrosylase GAPDH; Spermatogenic cell-specific glyceraldehyde 3-phosphate dehydrogenase 2; Spermatogenic glyceraldehyde-3-phosphate dehydrogenase

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Gene Aliases: BARS-38; CDABP0047; G3PD; GAPD; Gapd-s; GAPD2; GAPDH; GAPDH-2; GAPDH2; GAPDHS; GAPDS; HEL-S-162eP; HEL-S-278; HSD-35; HSD35; I79_001391; KNC-NDS6; OK/SW-cl.12

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UniProt ID: (Rabbit) P46406, (Human) P04406, (Chicken) P00356, (Human) O14556, (Mouse) P16858, (Chinese hamster) P17244, (Rat) P04797, (Rat) Q9ESV6, (Mouse) Q64467

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Entrez Gene ID: (Rabbit) 100009074, (Human) 2597, (Chicken) 374193, (Human) 26330, (Rabbit) 100352213, (Mouse) 14433, (Chinese hamster) 100736557, (Rat) 24383, (Rat) 66020, (Mouse) 14447, (Chinese hamster) 100767862

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glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity protein binding microtubule binding peptidyl-cysteine S-nitrosylase activity identical protein binding NADP binding NAD binding molecular_function oxidoreductase activity oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor

gluconeogenesis spermatid development sperm motility positive regulation of glycolytic process canonical glycolysis glucose metabolic process glycolytic process oxidation-reduction process microtubule cytoskeleton organization regulation of macroautophagy negative regulation of translation peptidyl-cysteine S-trans-nitrosylation protein stabilization neuron apoptotic process cellular response to interferon-gamma carbohydrate metabolic process apoptotic process multicellular organism development response to ammonium ion nuclear membrane fusion negative regulation of apoptotic process small molecule metabolic process regulation of translation

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