Phospho-c-Abl (Tyr89) (61A6) Rabbit mAb #3098

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 for 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 at Tyr245 is involved in the activation of c-Abl kinase (5). In addition, phosphorylation at Tyr412, which is located in the kinase activation loop of c-Abl, is required for kinase activity (6).
Phosphorylation of c-Abl on Tyr89 was identified at Cell Signaling Technology (CST) using PhosphoScan^®, CST's LC-MS/MS platform for phosphorylation site discovery as well as another publication using MS technology (7). For additional information please visit PhosphoSitePlus^®, CST's modification site knowledgebase, at www.phosphosite.org.