The c-Abl proto-oncogene encodes a nonreceptor type protein tyrosine kinase that is widely expressed and is distributed in both the nucleus and the cytoplasm of cells. It has been implicated in regulation of cell proliferation, differentiation, apoptosis, cell adhesion, and stress response. A variety of stimuli activate c-Abl kinase including integrin activation, PDGF stimulation, and binding to proteins, such as c-Jun. Tyrosine phosphorylation is important for the regulation of c-Abl kinase activity. Tyrosine 245 is located in the linker region between the SH2 and catalytic domains. Phosphorylation of Tyr-245 is involved in activation of c-Abl kinase activity. Tyrosine 412 is located in the kinase activation loop of c-Abl, and phosphorylation of this residue is required for kinase activity. Thus, phosphorylation of Tyr-245 and Tyr-412 may be critical for activation of c-Abl in a variety of cell signaling pathways.
References
Western blot analysis of K-562 cells treated with pervanadate (1 mM) for 30 minutes (lanes 1, 3, & 5). Some lanes were treated with alkaline phosphatase to remove phosphorylation on c-Abl (lanes 2, 4, & 6), then the blots were probed with anti-c-Abl (lanes 1 & 2), anti-c-Abl (Tyr-412) (AP1271; lanes 3 & 4), or anti-c-Abl (Tyr-245) (AP1251; lanes 5 & 6).
*For more information, see UniProt Accession P00519
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blotmobilities of known proteins with similar MW.
This kit contains:
