A non-radioactive method for the assay of many serine/threonine-specific protein kinases.
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.
Ross
Heike
H
Division of Signal Transduction Therapy, School of Life Sciences, University of Dundee, Scotland, UK.
Armstrong
Christopher G
CG
Cohen
Philip
P
D000818:Animals; D001331:Automation; D001671:Biochemistry / Q000379:methods*; D002460:Cell Line; D015195:Drug Design; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes; D004926:Escherichia coli / Q000201:enzymology; D007313:Insecta; D020935:MAP Kinase Signaling System; D010455:Peptides / Q000737:chemistry; D010766:Phosphorylation; D011485:Protein Binding; D047428:Protein Kinase Inhibitors; D017346:Protein Serine-Threonine Kinases / Q000032:analysis* / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity
D000939:Epitopes; D010455:Peptides; D047428:Protein Kinase Inhibitors; D017346:Protein Serine-Threonine Kinases