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

  • Heike Ross
  • , Christopher G. Armstrong
  • , Philip Cohen

Research output: Contribution to journalArticlepeer-review

33 Scopus citations

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.

Original languageEnglish
Pages (from-to)977-981
Number of pages5
JournalBiochemical Journal
Volume366
Issue number3
DOIs
StatePublished - 15 Sep 2002
Externally publishedYes

Keywords

  • Drug discovery
  • High-throughput screening
  • Peptide substrate
  • Phospho-specific antibody
  • Protein kinase inhibitor

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