Phospho-FAK (Tyr925) Rabbit anti-Human, Polyclonal, Bioss

Description

• Focal Adhesion Kinase (FAK) is a 125 kDa non-receptor protein tyrosine kinase that acts as a substrate for Src and is a key element of integrin signaling
• FAK plays an important role in cell spreading, differentiation, migration, cell death, and acceleration of the G1 to S phase transition of the cell cycle
• Tyrosine 397 is the autophosphorylation site of FAK, and involved in its initial activation
• This phosphorylated site binds Src family SH2 domains and the p85 subunit of PI3-Kinase, and activates cell migration and invasion
• FAK has a central catalytic domain and a C-terminal tail that localizes it to focal adhesions, which are sites where cells attach to the extracellular matrix via surface integrin receptors
• Increased FAK tyrosine phosphorylation occurs upon integrin engagement with fibronectin
• Adhesion of murine NIH3T3 fibroblasts to fibronectin promotes association of the Grb2 adapter protein and c-Src PTK with FAK in vivo, and also results in activation of the ERK2 MAP kinase
• In v-Src-transformed NIH3T3, the association of v-Src, Grb2, and Sos with FAK is independent of cell adhesion to fibronectin
• In vitro the Grb2 SH2 domain binds directly to tyrosine-phosphorylated FAK, and the binding site has been identified as Tyr925 by site directed mutagenesis
• Several transcript variants encoding different isoforms have been found for the FAK gene, but the full-length natures of only three of them have been determined.