Product Pathways - Tyrosine Kinase/ Adaptors
EphA1 Kinase #7709
Cell Signaling Technology offers a full line of protein kinases, substrates, antibody detection reagents and HTScan® kits. Browse our "Reagents for High-Throughput Screening" product listing or contact us at drugdiscovery@cellsignal.com.
Description
Purified recombinant kinase, supplied as a GST fusion protein.
Source / Purification
This GST-kinase fusion protein was produced using a baculovirus expression system with a construct expressing the kinase with an amino terminal GST tag. The protein was purified by one-step affinity chromatography using glutathione-agarose.
Quality Control
The purified kinase fusion protein was quality controlled for purity using SDS-PAGE followed by Coomassie or silver stain and Western blot. The specific activity of the kinase was determined using a radiometric assay.
Background
The Eph receptors are the largest known family of receptor tyrosine kinases (RTKs). They can be divided into two groups based on sequence similarity and on their preference for a subset of ligands: EphA receptors bind to a glycosylphosphatidylinositol-anchored ephrin A ligand, and EphB receptors bind to ephrin B proteins that have a transmembrane and cytoplasmic domain (1,2). Eph receptors and ligands may be involved in many diseases including cancer (3). Both ephrin A and ephrin B ligands have dual functions. As RTK ligands, the ephrins stimulate the kinase activity of the Eph receptors and activate signaling pathways in receptor-expressing cells. The ephrin extracellular domain is sufficient for this function as long as it is clustered (4). The second function of ephrins has been described as ?reverse signaling,? whereby the cytoplasmic domain becomes tyrosine phosphorylated, allowing interactions with other proteins that may activate signaling pathways in the ligand-expressing cells (5). Various stimuli can induce tyrosine phosphorylation of ephrin B, including binding to EphB receptors, activation of Src kinase and stimulation by PDGF and FGF (6). Tyrosines 324/327 have been identified as major phosphorylation sites of ephrin B1 in vivo (7).
- Wilkinson, D.G. (2000) Int. Rev. Cytol. 196, 177-244.
- Klein, R. (2001) Curr. Opin. Cell Biol. 13, 196-203.
- Dodelet, V.C. and Pasquale, E.B. (2000) Oncogene 19, 5614-5619.
- Holder, N. and Klein, R. (1999) Development 126, 2033-2044.
- Bruckner, K. et al. (1997) Science 275, 1640-1643.
- Palmer, A. et al. (2002) Mol. Cell 9, 1-20.
- Kalo, M.S. et al. (2001) J. Biol. Chem. 276, 38940-38948.
Application References
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