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Introduction to kinase assays
Kinases are enzymes which catalyze intracellular phosphorylation events- transfer of phosphate groups resulting from the conversion of adenosine triphosphate (ATP) into adenosine diphosphate (ADP).
Kinases are widely implicated into post-transcriptional maturation of proteins and intracellular signaling pathways. In mammalian cells, there are two main subdivisions of kinases based on their substrate specificity. As such, the protein tyrosine kinases (PTKs) phosphorylate their substrate on tyrosine residues, whereas the serine/threonine kinases (S/TKs) phosphorylate their substrate on serine or threonine residues. Further differentiations of kinase subfamilies are based on short amino acid stretches that characterize their binding and phosphorylation sites.
Protein kinases enzymes play a significant role in the control many of the key steps in cellular processes, such as signal transduction and cell cycle control. Consequently, kinase disorders are implicated in disease states such as cancer, atherosclerosis, psoriasis, and in inflammatory responses such as septic shock.
For these reasons, inhibitors that block the activity of protein kinases are potentially useful for the development of therapeutic agents.
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