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.
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Protein Aliases: aging-associated gene 9 protein; epididymis secretory sperm binding protein Li 162eP; G3PD; G3PDH; GAPD; GAPDH; Glyceraldehyde-3-Phosphate Dehydrogenase; Peptidyl-cysteine S-nitrosylase GAPDH
Gene Aliases: CDABP0047; G3PD; GAPD; GAPDH; HEL-S-162eP; OK/SW-cl.12