Anti-GAPDH

GAPDH (Glyceraldehyde-3-Phosphate Dehydrogenase) is an enzyme best known for its role in glycolysis. However, extra-glycolytic functions of GAPDH have been described, including regulation of protein expression via RNA binding. GAPDH binds to numerous AREs (adenine-uridine rich elements) from various mRNA untranslated regions in vitro and in vivo despite its lack of a canonical RNA binding motif. GAPDH specifically catalyzes the simultaneous phosphorylation and oxidation of glyceraldehyde 3-phosphate using NAD+ (Nicotinamide Adenine Dinucleotide) as a cofactor to produce glycerate 1,3-biphosphate and NADH. In addition to its role in energy production, GAPDH has been implicated in many cellular processes including DNA repair tRNA export, membrane fusion and transport, endocytosis and nuclear membrane assembly, and cell death. Protein function: Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC. Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D- glyceroyl phosphate. Component of the GAIT (gamma interferon- activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation. [The UniProt Consortium]