Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is a metabolic enzyme responsible for catalyzing one step in the glycolytic pathway, the reversible oxidative phosphorylation of glyceraldehyde 3-phosphate to produce glyceraldehyde 1-3-bisphosphate. Because GAPDH protein is expressed in large amounts and is required at all times for an important “house keeping” function, levels of GAPDH mRNA are often measured and used as standards in studies of the expression of other mRNAs. Similarly specific antibodies to GAPDH are used to measure GAPDH expression as a protein standard in western blotting experiments, allowing comparison between the level of this protein and others in a cell or tissue.
This antibody was raised against extensively purified pig GAPDH. The antibody has been widely used as a western blotting standard by many labs for many years and is known to detect GAPDH in a variety of mammalian species including human, rat and mouse. Current data suggests that the epitope for the antibody is within the peptide KYDDIKKVVKQASEGPLKGI, amino acids 254-273 of the human sequence, a peptide which is highly conserved across mammalian species. The antibody produces a single clean band on western blots of typical cell and tissue extracts.
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