Phospho-c-Abl (Thr735) Antibody detects endogenous levels of c-Abl or Bcr-Abl only when phosphorylated at threonine 735. The antibody does not cross-react with other related proteins.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with synthetic phosphopeptide corresponding to residues surrounding Thr735 of human c-Abl. Antibodies are purified by protein A and peptide affinity chromatography.
Background
The c-Abl proto-oncogene encodes a nonreceptor protein tyrosine kinase that is ubiquitously expressed and highly conserved in metazoan evolution. c-Abl protein is distributed in both the nucleus and the cytoplasm of cells. It is implicated in regulating cell proliferation, differentiation, apoptosis, cell adhesion and stress responses (1-3). c-Abl kinase activity is increased in vivo by diverse physiological stimuli including integrin activation, PDGF stimulation and binding to c-Jun, Nck and RFX1 (2,4). The in vivo mechanism of regulation of c-Abl kinase activity is not completely understood. Tyr245 is located in the linker region between the SH2 and catalytic domains. This positioning is conserved among Abl family members. Phosphorylation of Tyr245 is involved in the activation of c-Abl kinase (5). In addition, phosphorylation of Tyr412, which is located in the kinase activation loop of c-Abl, is required for kinase activity (6).Thr735 is located within a conserved 14-3-3 protein binding motif region, and can be phosphorylated upon stress stimulation or TPA treatment. Phosphorylation at Thr735 may play an important role in regulating c-Abl localization as well as its function.