C-Abl (Tyr-412), Phosphospecific Antibody

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

This antibody was cross-adsorbed to phospho-tyrosine coupled to agarose and to phospho-c-Abl (Tyr-245) peptide before affinity purification using phospho-c-Abl (Tyr-412) peptide. On SDS-PAGE immunoblots of K-562 treated with pervanadate the antibody detects a 145 kDa* protein corresponding to c-Abl and a 210 kDa band corresponding to BCR-Abl. This peptide sequence has high homology to the conserved site in rat and mouse c-Abl, as well as in viral Abl and BCR-Abl fusion protein.