Anti-GAPDH Antibody Picoband® Fluoro488 Conjugated

Glyceraldehyde 3-phosphate dehydrogenase (abbreviated as GAPDH or less commonly as G3PDH) is an enzyme of ~37kDa that catalyzes the sixth step of glycolysis and thus serves to break down glucose for energy and carbon molecules. This gene encodes a member of the glyceraldehyde-3-phosphate dehydrogenase protein family. GAPDH is mapped to 12p13.31. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. The product of this gene catalyzes an important energy-yielding step in carbohydrate metabolism, the reversible oxidative phosphorylation of glyceraldehyde-3-phosphate in the presence of inorganic phosphate and nicotinamide adenine dinucleotide (NAD) . The encoded protein has additionally been identified to have uracil DNA glycosylase activity in the nucleus.

E.coli-derived human GAPDH recombinant protein (Position: N136-E335) . Human GAPDH shares 95% and 94.5% amino acid (aa) sequence identity with mouse and rat GAPDH, respectively.

Alzheimer's Disease, Cancer, Cancer Metabolism, Carbohydrate Metabolism, Energy Metabolism, Energy Transfer Pathways, Metabolic Signaling Pathway, Metabolic Signaling Pathways, Metabolism, Metabolism Of Carbohydrates, Neurodegenerative Disease, Neurology Process, Neuroscience, Pathways and Processes, Signal Transduction

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 (By similarity) . 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. .

1. Bae, B.-I., Hara, M. R., Cascio, M. B., Wellington, C. L., Hayden, M. R., Ross, C. A., Ha, H. C., Li, X.-J., Snyder, S. H., Sawa, A. Mutant Huntingtin: nuclear translocation and cytotoxicity mediated by GAPDH. Proc. Nat. Acad. Sci. 103: 3405-3409, 2006. 2. Colell, A., Ricci, J.-E., Tait, S., Milasta, S., Maurer, U., Bouchier-Hayes, L., Fitzgerald, P., Guio-Carrion, A., Waterhouse, N. J., Li, C. W., Mari, B., Barbry, P., Newmeyer, D. D., Beere, H. M., Green, D. R. GAPDH and autophagy preserve survival after apoptotic cytochrome c release in the absence of caspase activation. Cell 129: 983-997, 2007. Note: Erratum: Cell 130: 385 only, 2007. 3. Tarze A, Deniaud A, Le Bras M, Maillier E, Molle D, Larochette N, Zamzami N, Jan G, Kroemer G, Brenner C (April 2007) . GAPDH, a novel regulator of the pro-apoptotic mitochondrial membrane permeabilization.Oncogene 26 (18) : 2606–20.

Cytoplasm, cytosol . Nucleus . Cytoplasm, perinuclear region . Membrane . Cytoplasm, cytoskeleton . Translocates to the nucleus following S- nitrosylation and interaction with SIAH1, which contains a nuclear localization signal (By similarity) . Postnuclear and Perinuclear regions. .