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. 2002 Sep 15;366(Pt 3):977–981. doi: 10.1042/BJ20020786

A non-radioactive method for the assay of many serine/threonine-specific protein kinases.

Heike Ross 1, Christopher G Armstrong 1, Philip Cohen 1
PMCID: PMC1222845  PMID: 12119045

Abstract

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.

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Selected References

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