Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), also called uracil DNA glycosylase, catalyzes the reversible oxidative phosphorylation of glyceraldehyde-3-phosphate in the presence of inorganic phosphate and nicotinamide adenine dinucleotide (NAD), an important energy-yielding step in carbohydrate metabolism. While GAPDH has long been recognized as playing an integral role in glycolysis, additional functions of GAPDH include acting as a uricil DNA glycosylase, activating transcription, binding RNA and involvement in nuclear RNA export, DNA replication and DNA repair. Expression of GAPDH is upregulated in liver, lung and prostate cancers. GAPDH translocates to the nucleus during apoptosis. GAPDH complexes with neuronal proteins implicated in human neuro-degenerative disorders including the beta-Amyloid precursor, Huntingtin and other triplet repeat neuronal disorder proteins.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB: 1:500~1:1000
Application Notes:
GAPDHS polyclonal antibody detects endogenous levels of GAPDHS protein.
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