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 the "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 Tyr577) 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.
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注意事项:
1.Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2.Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
3.This antibody has been developed and certified for the bioimaging application. However, a routine bioimaging test is not performed on every lot. Researchers are encouraged to titrate the reagent for optimal performance.