Fak (Py397) (Focal Adhesion Kinase (Py397)) Mouse Anti-Human, Unlabeled, Clone: 18, Bd, Mouse Monoclonal Antibody, Each

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Focal adhesion kinase (fak) is a cytoplasmic tyrosine kinase that colocalizes with integrins in focal adhesions. This cellular localization is directed by a 125 amino acid sequence at the c-terminus called “focal adhesion targeting” sequence (fat). The binding of extracellular matrix ligands to integrins triggers autophosphorylation at tyr-397, and activation of fak through phosphorylation of tyr residues (tyr-576 and tyr-577) in the kinase domain activation loop. For example, cell adhesion to a fibronectin substratum involves concurrent activation of src and phosphorylation of the fak activation loop. In addition, phosphorylation of other tyr residues (tyr-925 and tyr-861) creates binding sites for sh2 domains of intracellular signaling molecules such as src, pi3 kinase, and grb2. Fak's ability to bind numerous structural and signaling proteins via a variety of interactions is important for fak activation level and for fak interaction with a variety of substrates localized to sites of cell adhesion. Thus, fak activity is regulated by a complex set of phosphorylation sites, and this phospho-regulation could be important for cell motility, cell growth, cytoskeletal organization and adhesion-dependent cell survival.Host species: mouseclone: 18isotype: igg1species reactivity [for features main]: humanimmunogen: human fak (py397)bioimaging, immunofluorescence, western blotting