Non-receptor protein-tyrosine kinase implicated in signaling pathways involved in cell motility, proliferation and apoptosis. Activated by tyrosine-phosphorylation in response to either integrin clustering induced by cell adhesion or antibody cross-linking, or via G-protein coupled receptor (GPCR) occupancy by ligands such as bombesin or lysophosphatidic acid, or via LDL receptor occupancy. Microtubule-induced dephosphorylation at Tyr-397 is crucial for the induction of focal adhesion disassembly. Plays a potential role in oncogenic transformations resulting in increased kinase activity.1) Matsuya M. et. al. (1998) J. Biol. Chem. 273:1003-1014Fujita H. et. al. (1998) J. Biol. Chem. 273:26516-26521Le Romancer M. et. al. (2008) Mol. Cell 31:212-221
Immunogen
FAK (Phospho-Tyr397) antibody was raised against a peptide sequence around phosphorylation site of tyrosine 397 (D-D-Y (p) -A-E) derived from Human FAK.