Anti-Pyruvate Kinase / PKM2

0.5mg/ml if reconstituted with 0.2ml sterile DI water. PKM (Pyruvate Kinase, Muscle), also known as PK3 or PKM2, is an enzyme that in humans is encoded by the PKM gene. The activity of pyruvate kinase subtype M2 is increased by fructose 1, 6-bisphosphate (Fru-1, 6-P2). By in situ hybridization, Popescu and Cheng (1990) mapped the THBP1 gene to 15q24-q25. Ashizawa et al. (1991) manipulated the intracellular Fru-1, 6-P2 concentration in several mammalian cell lines, including human, by varying the glucose concentration in the media. Using a novel proteomic screen for phosphotyrosine-binding proteins, Christofk et al. (2008) observed that PKM2 binds directly and selectively to tyrosine-phosphorylated peptides. Protein function: Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP (PubMed:20847263, PubMed:15996096, PubMed:1854723). The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production (PubMed:20847263, PubMed:15996096, PubMed:1854723). The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival (PubMed:20847263, PubMed:15996096, PubMed:1854723). [The UniProt Consortium]