Anti-GAPDH

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is an enzyme that catalyzes the conversion of glyceraldehyde-3-phosphate (Cay-17865) to 1,3-bisphosphoglycerate during glycolysis and is involved in numerous additional cellular processes, including intracellular trafficking, receptor-mediated signaling, apoptosis, DNA repair, and the oxidative stress response. It exists as a tetramer and is composed of an N-terminal domain, which contains binding sites for NAD+, phosphatidylserine, RNA, and glutathione, and a C-terminal catalytic domain. GAPDH is widely expressed and primarily localizes to the cytosol, where it has roles in glycolysis and intracellular trafficking. It also localizes to the nucleus, mediating DNA integrity, gene transcription, and apoptosis, as well as to cellular membranes, where it has roles in membrane fusion and iron transport. GAPDH expression is increased by insulin, hypoxia-inducible factor-1 (HIF-1), p53, and nitric oxide (NO) and decreased by acetylated histones. Aberrant mRNA and protein levels of GAPDH have been found in tumor biopsies from patients with a variety of cancers, including lung, renal cell, colorectal, or breast cancer. Cayman's GAPDH Monoclonal Antibody can be used for immunocytochemistry (ICC), immunoprecipitation (IP), chromatin immunoprecipitation (ChIP), and Western blot (WB) applications. The antibody recognizes GAPDH at approximately 36 kDa.