Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is well-known as one of the key enzymes involved in glycolysis. It catalyzes the reversible oxidative phosphorylation of glyceraldehydes-3-phosphate. Besides functioning as a glycolytic enzyme in cytoplasm, recent evidence suggest that mammalian GAPDH is also involved in a great number of intracellular processes such as membrane fusion, microtubule bundling, phosphotransferase activity, nuclear RNA export, DNA replication and repair. During the last decades many findings have been made concerning the role of GAPDH in different pathologies including prostate cancer progression, programmed neuronal cell death and age-related neuronal diseases such as Alzheimer’s and Huntington’s diseases.
GAPDH molecule is a homotetramer composed of 36 kDa subunits. Thus the molecular weight for the whole molecule is 144 kDa. Since it is constitutively and stably expressed in almost all tissues at high level, GAPDH became a well-established “housekeeping” protein and is widely used as a loading control for protein normalization in such procedures as Western blotting. It is also useful for cells visualizing in microscopy assays. Some physiological factors, such as hypoxia and diabetes, can increase GAPDH expression in certain cell types.
Anti-GAPDH monoclonal antibodies developed by HyTest, especially well characterized MAb 6C5, are suitable for GAPDH immunodetection in Western blotting, sandwich immunoassays and immunocytochemical applications.
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