The generation of drugs that modulate the activities of particular protein kinases has become a prime focus of the pharmaceutical and biotechnology industry. Consequently, improved methods for the development of high-throughput screening formats for these enzymes is a high priority. In the present study, we have designed three generic peptide substrates that can be used to assay a diverse range of protein kinases. These peptides share a common seven-residue epitope that includes the site of phosphorylation, and against which we have generated a phospho-specific antibody. Thus a large number of serine/threonine-specific protein kinases can be screened using a simple non-radioactive format.
A non-radioactive method for the assay of many serine/threonine-specific protein kinases
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Heike ROSS, Christopher G. ARMSTRONG, Philip COHEN; A non-radioactive method for the assay of many serine/threonine-specific protein kinases. Biochem J 15 September 2002; 366 (3): 977–981. doi: https://doi.org/10.1042/bj20020786
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