Merck UK: Recombinant Active Protein Kinases

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Recombinant Active Protein Kinases

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Protein phosphorylation corresponds to one of the most important molecular mechanisms by which extracellular signals produce their biological responses in cells. Stimulation of protein kinases is considered to be one of the most common activation mechanisms in signal transduction systems. Protein phosphorylation systems are composed of at least three components: (a) phosphoproteins, that alter their properties during phosphorylation-dephosphorylation; (b) protein kinases, that transfer a phosphate group from ATP to specific serine, threonine, or tyrosine residues on proteins; and (c) protein phosphatases, that dephosphorylate the phosphoproteins, thereby restoring the particular protein phosphorylation system to its basal stage. The eukaryotic protein kinases, by virtue of their catalytic domains constitute one of the largest super-families of homologous proteins that are related. Most protein kinases are specific for either serine/threonine or tyrosine phosphorylation and possess a 30-32 kDa catalytic domain that is well conserved throughout the phylogeny. These sequences share a large number of residues involved in ATP binding, catalysis, and maintenance of structural integrity.

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Active Protein Kinases

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Recombinant Proteins: Protein Kinases & Phosphatases

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