Kinase(s)

Protein phosphorylation is a key aspect in the regulation of a large number of cellular processes including cellular division, metabolism, signal transduction, and many more. There are over 500 kinases encoded by the human genome and it has been estimated that kinases regulate approximately 50% of cellular functions. Kinase is the name given to an enzyme that catalyzes the transfer of a phosphate group from ATP to another molecule. Kinases can be broadly separated by their substrate into protein and lipid kinases with the protein kinases being further classified based on their cellular location and the specific amino acid(s) they phosphorylate; cytoplasmic threonine, receptor tyrosine kinases (RTKs), and serine/threonine.

The prominent roles that kinases play in cell division have made them attractive targets for both immunosuppressant drugs and cancer therapeutics. Kinases are highly druggable, and account for over 25% of targets screened by the pharmaceutical industry. Currently, there are over 25 kinase inhibitors that have been approved for clinical use by the FDA, including rapamycin, which was discovered in the 1960s. It was not until three decades later, however, that the target of rapamycin was discovered to be a serine/threonine kinase that was named mammalian target of rapamycin (mTOR). Today rapamycin is approved as an immunosuppressant and a number of mTOR inhibitors are being investigated as treatments for various forms of cancer.

BPS offers a wide selection of kinases, kinase substrates and kinase inhibitors. Our kinases are validated through rigorous QC testing and are suitable for use in nearly all in vitro kinase assays. We also offer kinase inhibitor screening services.

References:

1.   Cohen, P. Nat. Rev. Drug Disc. 2002; 1: 309-315.
2.   Ballou, L.M., et al., J. Chem. Biol. 2008 1(1-4): 27-36.
3.   Loewith, R., et al., Genetics. 2011; 189(4): 1177-1201.