Anti-PKM2 Antibody Picoband® Fluoro647 Conjugated

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 ly and selectively to tyrosine-phosphorylated peptides.

Pyruvate kinase PKM;2.7.1.40; Cytosolic thyroid hormone-binding protein; CTHBP; Opa-interacting protein 3; OIP-3; Pyruvate kinase 2/3; Pyruvate kinase muscle isozyme; Thyroid hormone-binding protein 1; THBP1; Tumor M2-PK; p58; PKM; OIP3, PK2, PK3, PKM2

A synthetic peptide corresponding to a sequence at the N-terminus of human PKM2, different from the related mouse sequence by five amino acids, and from the related rat sequence by four amino acids.

Cancer, Cancer Metabolism, Carbohydrate Metabolism, Cell Cycle, Energy Metabolism, Energy Transfer Pathways, Epigenetics and Nuclear Signaling, Kinases/Phosphatases, Metabolic Signaling Pathway, Metabolic Signaling Pathways, Metabolism, Metabolism Of Carbohydrates, Pathways and Processes, Signal Transduction, Tumor Biomarkers

Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation. Plays a general role in caspase independent cell death of tumor cells. The ratio betwween 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. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival. .

1. Ashizawa, K., Willingham, M. C., Liang, C.-M., Cheng, S. In vivo regulation of monomer-tetramer conversion of pyruvate kinase subtype M-2 by glucose is mediated via fructose 1, 6-bisphosphate. 2. J. Biol. Chem. 266: 16842-16846, 1991. 2. Christofk, H. R., Vander Heiden, M. G., Wu, N., Asara, J. M., Cantley, L. C. Pyruvate kinase M2 is a phosphotyrosine-binding protein. 3. Nature 452: 181-186, 2008. 3. Popescu, N. C., Cheng, S. Y. Chromosomal localization of the gene for a human cytosolic thyroid hormone binding protein homologous to the subunit of pyruvate kinase, subtype M (2) . Somat. Cell Molec. Genet. 16: 593-598, 1990.

Cytoplasm. Nucleus. Translocates to the nucleus in response to different apoptotic stimuli. Nuclear translocation is sufficient to induce cell death that is caspase independent, isoform-specific and independent of its enzymatic activity.