mouse monoclonal IgG1; GAPDH Antibody (G-9) is an IgG1 κ mouse monoclonal GAPDH antibody that detects GAPDH and GAPDH-2 of mouse, rat and human origin by WB, IP, IF, IHC(P) and ELISA. GAPDH Antibody (G-9) is available as the non-conjugated anti-GAPDH antibody form, as well as multiple conjugated forms of anti-GAPDH antibody, including agarose, HRP, PE, FITC and multiple Alexa Fluor® conjugates. GAPDH Antibody (G-9) specifically detects Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), also called uracil DNA glycosylase. The GAPDH protein 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, suggesting these tissues are suitable positive controls for the GAPDH Antibody (G-9). GAPDH translocates to the nucleus during apoptosis. Thus, immunostaining by the GAPDH Antibody (G-9) may result in either cytoplasmic or nuclear localization. GAPDH complexes with neuronal proteins implicated in human neuro-degenerative disorders including the β-Amyloid precursor, Huntingtin and other triplet repeat neuronal disorder proteins.