Human phospho-FAK (Y925) Antibody

Focal adhesion kinase 1 (FAK) is a ubiquitously expressed non-receptor protein tyrosine kinase that is concentrated in the focal adhesions that form between cells growing in the presence of extracellular matrix constituents. This cellular localization is directed by a "Focal Adhesion Targeting" (FAT) sequence, a 125 amino acid sequence at the C-terminus. FAK plays an important role in migration, cell spreading, differentiation, cytoskeleton protein phosphorylation, apoptosis and acceleration of the G1 to S phase transition of the cell cycle. It associates with several different signaling proteins such as Src-family PTKs, p130Cas, Shc, Grb2, PI 3-kinase, and paxillin. This enables FAK to function within a network of integrin-stimulated signaling pathways leading to the activation of targets such as the ERK and JNK/mitogen-activated protein kinase pathways. FAK is also linked to oncogenes at biochemical and functional levels. Increased expression and/or activity of FAK in various tumors has been correlated with enhanced migration and invasiveness of human tumor cells in addition to promoting increased cell proliferation.