c-Abl Antibody detects endogenous levels of Abl proteins.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the sequence close to the carboxy-terminus 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).