|Other Names||Pyruvate kinase PKM, 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|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Synonyms||OIP3, PK2, PK3, PKM2|
|Function||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 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. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival.|
|Cellular Location||Cytoplasm. Nucleus. Note=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|
|Tissue Location||Specifically expressed in proliferating cells, such as embryonic stem cells, embryonic carcinoma cells, as well as cancer cells.|
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Provided below are standard protocols that you may find useful for product applications.
PKM2 is a pyruvate kinase that catalyzes the production of phosphoenolpyruvate from pyruvate and ATP. This protein has been shown to interact with thyroid hormone, and thus may mediate cellular metabolic effects induced by thyroid hormones. This protein has been found to bind Opa protein, a bacterial outer membrane protein involved in gonococcal adherence to and invasion of human cells, suggesting a role of this protein in bacterial pathogenesis.
Lehner, B., et al., Genome Res. 14(7):1315-1323 (2004).Gevaert, K., et al., Nat. Biotechnol. 21(5):566-569 (2003).Valentini, G., et al., J. Biol. Chem. 277(26):23807-23814 (2002).Lowrie, D.J. Jr., et al., J. Struct. Biol. 132(2):83-94 (2000).Williams, J.M., et al., Mol. Microbiol. 27(1):171-186 (1998).
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