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

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

  • Biochem J. 2002 Sep 15;366(Pt 3):977-81. doi: 10.1042/BJ20020786.
Heike Ross 1 Christopher G Armstrong Philip Cohen
Affiliations

Affiliation

  • 1 Division of Signal Transduction Therapy, School of Life Sciences, University of Dundee, Scotland, UK.
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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