Pyruvate kinase (EC: 2.7.1.40) is an enzyme involved in glycolysis. It catalyzes the transfer of a phosphate group from phosphoenolpyruvate (PEP) to ADP, yielding one molecule of pyruvate and one molecule of ATP. This process also requires a magnesium ion. The enzyme is a 'transferase' under the international classification of enzymes. This step is the final one in the glycolytic pathway, which produces pyruvate molecules, the final product of aerobic glycolysis. However, in anaerobic glycolysis, lactate dehydrogenase will utilize the NADH produced by glyceraldehyde phosphate dehydrogenase to reduce pyruvate to lactate. In humans, there are two pyruvate kinase isozymes: type M (muscle, SwissProt P14618) and type L,R (liver and erythrocyte, SwissProt P30613). The isozymes differ in primary structure and regulation. This reaction has a large positive free energy change, one of three in glycolysis. All three such steps regulate the overall activity of the pathway, and are, in general, irreversible under wild-type conditions. Anti-Pyruvate kinase antibody is idea for investigators involved in cytokines and growth factor research.
Store vial at 4° C prior to restoration.?? For extended storage aliquot contents and freeze at -20° C or below.? Avoid cycles of freezing and thawing.? Centrifuge product if not completely clear after standing at room temperature.? This product is stable for several weeks at 4° C as an undiluted liquid.? Dilute only prior to immediate use.