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Glyceraldehyde 3-Phosphate Dehydrogenase (GAPDH) is a metabolic enzyme responsible for catalyzing one step in the glycolytic pathway, the reversible oxidative phosphorylation of glyceraldehyde 3-phosphate. Because GAPDH is a protein expressed in large amounts and which is required at all times for important "house keeping" functions, levels of GAPDH mRNA are often measured and used as standards in studies of mRNA expression. Increasingly, scientists are making use of specific antibodies to GAPDH in comparable studies of levels of protein expression. 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, and the polyglutamine tracts of Huntingtin, the protein product aberrant forms of which are causative of Huntington's disease. Associations with actin and tubulin have also been reported. The protein may also have a role in the regulation of apoptosis, and interestingly migrates from the cytoplasm into the nucleus when cells become apoptotic.
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Protein Aliases: epididymis secretory protein Li 278; GAPDH S; GAPDH-2; Glyceraldehyde-3-phosphate dehydrogenase, testis-specific; Spermatogenic cell-specific glyceraldehyde 3-phosphate dehydrogenase 2; Spermatogenic glyceraldehyde-3-phosphate dehydrogenase
Gene Aliases: GAPD2; GAPDH-2; GAPDH2; GAPDHS; GAPDS; HEL-S-278; HSD-35; HSD35
UniProt ID: (Human) O14556
Entrez Gene ID: (Human) 26330
Molecular Function: dehydrogenase