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 Citations (Scopus)

    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
    Publication statusPublished - 15 Sep 2002

    Keywords

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

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