Sino Biological offers a comprehensive set of tools for protein kinase related research, including recombinant proteins, antibodies, ELISA kits, and cDNA clones.
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Protein kinases modify their target proteins by transferring phosphate groups from ATP to serine, threonine, or tyrosine residues on them (phosphorylation). Phosphorylation usually results in a functional change of the substrate by changing enzyme activity, intracellular location, or association with other proteins. Protein kinases are particularly prominent in signal transduction and are known to regulate the majority of cell processes, such as cell growth, differentiation, metabolism, gene transcription, and so on. Most kinases act on both serine and threonine, others act on tyrosine, and a number act on all three. Serine/threonine protein kinases phosphorylate the OH group of serine or threonine amino acid residues. These protein kinases are usually stimulated by numerous chemical signals, including cAMP/cGMP, Ca2+/calmodulin, diacylglycerol. Tyrosine-specific protein kinases that phosphorylate tyrosine amino acid residues act primarily as growth factor receptors and in downstream signaling from growth factors. Abnormal activity of protein kinases is a frequent cause of disease, particularly cancer. Protein kinases have emerged as one of the most frequently targeted families of proteins in drug discovery. The development of small-molecule inhibitors that have the potency and selectivity necessary to be effective cancer drugs has gained notable successes over the past decades.