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Anti-GAPDH Antibody

from rabbit, purified by affinity chromatography

glyceraldehyde 3-phosphate dehydrogenase, aging-associated gene 9 protein, glyceraldehyde-3-phosphate dehydrogenase, GAPDH, G3PDH, GAPD, OK/SW-cl.12, MGC88685, G3PD, EC

biological source


Quality Level

antibody form

affinity isolated antibody

antibody product type

primary antibodies



purified by

affinity chromatography

species reactivity

human, rat, mouse

species reactivity (predicted by homology)

bovine (based on 100% sequence homology), guinea pig (based on 100% sequence homology)


western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

General description

Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is an ubiquitous glycolytic enzyme present in moderately high levels in almost all tissues. As a ′house-keeping′ enzyme, it catalyzes the synthesis of 1,3-biphosphoglycerate, a "high energy" intermediate used for the synthesis of ATP. Besides its cytoplasmic action in metabolism it is also involved in the initial stages of apoptosis or oxidative stress response where GAPDH is translocated to the nucleus. Such actions may reflect the role of GAPDH in DNA repair or as one nuclear carrier for apoptotic molecules. GAPDH has also been found to bind specifically to proteins implicated in the pathogenesis of a variety of neurodegenerative disorders including the beta-amyloid precursor protein and the huntingtin protein where decreased function of GAPDH is associated with Alzheimer′s and Huntington′s disease fibroblasts. GAPDH has also been identified as a potential target for nitric oxide (NO)-mediated cellular toxicity. The complete and functional enzyme is a tetramer with each of four identical subunits occupying the vertex of a tetrahedron. Binding domains also include one principally interacting with NAD+ and another interacting with glyceraldehyde 3-phosphate (GAP).


This antibody recognizes GAPDH at the C-terminus.


Epitope: C-terminus
GST-tagged recombinant protein corresponding to the C-terminus of human GAPDH.


Research Category
Anti-Glyceraldehyde-3-Phosphate Dehydrogenase Antibody is popular affinity purified polyclonal antibody. This antibody is supported by peer reviewed publications and reliably detects Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) is validated for use in WB.


Evaluated by Western Blot in HEK293 cell lysate.

Western Blot Analysis: 0.5 µg/mL of this antibody detected GAPDH on 10 µg of HEK293 cell lysate.

Target description

~36kDa observed

Physical form

Purified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Affinity purified

Storage and Stability

Stable for 1 year at 2-8°C from date of receipt.

Analysis Note

HEK293 cell lysate

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.


Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage Class Code

12 - Non Combustible Liquids



Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Certificate of Origin

Takeru Sugihara et al.
British journal of cancer, 114(9), 1012-1018 (2016-03-24)
Recent Drosophila studies showed that Discs-large (Dlg) is critical for regulation of cell polarity and tissue architecture. We investigated the possibility that loss of the human homologue of Drosophila Dlg (DLG1) is involved in endometrial carcinogenesis. We analysed DLG1 expression
Mitochondrial peroxiredoxin 3 regulates sensory cell survival in the cochlea.
Chen, FQ; Zheng, HW; Schacht, J; Sha, SH
Testing null
Jun Chen et al.
Journal of the Association for Research in Otolaryngology : JARO, 17(4), 289-302 (2016-04-21)
Loss of auditory sensory hair cells is the major pathological feature of noise-induced hearing loss (NIHL). Currently, no established clinical therapies for prevention or amelioration of NIHL are available. The absence of treatments is due to our lack of a
Minal Patel et al.
PloS one, 8(3), e58471-e58471 (2013-03-09)
Acoustic trauma, one of the leading causes of sensorineural hearing loss, induces sensory hair cell damage in the cochlea. Identifying the molecular mechanisms involved in regulating sensory hair cell death is critical towards developing effective treatments for preventing hair cell
Gabriela G Chavez et al.
Nitric oxide : biology and chemistry, 71, 27-31 (2017-10-17)
Experimental work over the past several years has revealed an unexpected abundance of long natural antisense transcripts (NATs) in eukaryotic species. In light of the proposed role of such RNA molecules in the regulation of gene expression in the brain

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