Choosing the Best Kinase Assay to Meet Your Research Needs

Content Provider	Semantic Scholar
Author	Curtin, Michael
Copyright Year	2005
Abstract	11 CELL NOTES ISSUE 13 2005 C LL IG N A IN G Introduction Protein kinases are enzymes capable of transferring the γphosphate group from ATP to a serine, threonine or tyrosine residue in specific substrate proteins. These phosphorylation events modulate the activity of a vast number of proteins, including ion channels, transcription factors, phosphatases and other kinases. Based on sequence analysis, the human genome encodes approximately 518 protein kinases, and approximately one-third of the proteins in a typical mammalian cell are phosphorylated (1). Protein kinases function primarily as components of signaling pathways in which signals perceived at the surface of a cell are transduced through the cell by a series phosphorylation events that ultimately bring about a cellular response, such as a change in the rate of gene transcription or the modulation of ion channel activity. Protein kinases play critical roles in a variety of cellular functions including cell growth, development, differentiation, membrane transport, and cell death (2,3). Abnormalities in signaling pathways can lead to various pathological conditions including many forms of cancer. For this reason, protein kinases are important targets for both basic research and drug development.
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