FAK [pY397] ELISA recognizes human, rat, and mouse FAK. Other species have not been tested. The specificity of this assay for phosphorylated FAK [pY397] was confirmed by peptide competition. The data show that only the phospho-peptide containing the phosphorylated tyrosine 397 could block the ELISA signal. The non-phosphorylated peptide sequence or other phosphopeptides from the FAK sequence did not block the signal.
Sensitivity
> 1 U/mL
Characteristics
FAK, phosphorylated (Tyr397), Human (Focal Adhesion Associated Protein Tyrosine Kinase, BC3) ELISA Kit
FAK (PTK2)
(PTK2 Protein tyrosine Kinase 2 (PTK2))
Alternative Name
FAK
Background
Focal Adhesion Kinase (FAK), also known as pp125FAK and FADK 1 (EC,2.7.1.112) is a non-receptor protein-tyrosine kinase that localizes to focal adhesions. FAK appears to be ubiquitously expressed among all mammalian tissues, with highest expression levels observed in brain tissue. FAK plays a central role in cell spreading, differentiation, migration, cell death and acceleration of the G1 to S phase transition of the cell cycle. FAK's amino-terminal, which bears homology with the band 4.1 family of proteins, plays a role in mediating interaction with the cell membrane, the cytoskeleton, and integrin proteins. FAK's carboxyl-terminus, which contains the focal adhesion targeting (FAT) domain, mediates interaction with focal adhesion associated proteins, including talin and paxillin. FAK is activated by phosphorylation events in response to several stimuli. These stimuli include integrin clustering induced by cell adhesion or antibody cross-linking, G-protein coupled receptor (GPCR) occupancy by ligands such as bombesin or lysophosphatidic acid, or by LDL receptor occupancy.