GAPDH Antibody – Mouse Monoclonal

This gene encodes a member of the glyceraldehyde-3-phosphate dehydrogenase protein family. A similar protein in human and mouse has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. The encoded protein was originally identified as a key glycolytic enzyme that converts D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Subsequent studies in human and mouse have assigned a variety of additional functions to the protein including nitrosylation of nuclear proteins. Many pseudogenes similar to this locus are found throughout the rat genome. [provided by RefSeq, Jan 2014]

GAPDH: a multifunctional enzyme with both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities. A key glycolytic enzyme that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. An important enzyme for energy metabolism, and the production of ATP and pyruvate through anaerobic glycolysis in the cytoplasm. Additionally, it participates in apoptosis, membrane trafficking, iron metabolism, nuclear activities and receptor mediated cell signaling. Its subcellular localization changes reflecting its multiple activities. Is cytosolic, but is also localized in the membrane, the nucleus, polysomes, the ER and the Golgi. Participates in transcription, RNA transport, DNA replication and apoptosis. S-nitrosylation on Cys-152 following apoptotic stimulates its interaction with SIAH2, which in turn moderates its translocation into the nucleus. Mediates cysteine S-nitrosylation of nuclear target proteins including SIRT1, HDAC2 and DNA-PK. Deregulated in lung cancer, renal cancer, breast cancer, gastric cancer, glioma, liver cancer, colorectal cancer, melanoma, prostatic cancer, pancreatic cancer and bladder cancer. Its increased expression and enzymatic activity is associated with cell proliferation and tumorigenesis, Oxidative stress impairs GAPDH catalytic activity and leads to cellular aging and apoptosis. In experimental animal models, injection of GAPDH antagonists induces apoptosis and blocks Hep3B tumor progression, suggesting a therapeutic potential of targeting GAPDH in human hepatocellular carcinoma

Protein type: Oxidoreductase; Carbohydrate Metabolism - glycolysis and gluconeogenesis; EC 1.2.1.12

Cellular Component: microtubule cytoskeleton; nuclear membrane; mitochondrion; membrane; intracellular membrane-bound organelle; cytoplasm; plasma membrane; lipid particle; ribonucleoprotein complex; nucleus; cytosol; vesicle

Molecular Function: identical protein binding; protein binding; microtubule binding; glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity; NADP binding; NAD binding

Biological Process: regulation of translation; neuron apoptosis; glycolysis; protein stabilization; apoptosis; negative regulation of translation; multicellular organismal development; carbohydrate metabolic process; microtubule cytoskeleton organization and biogenesis; gluconeogenesis