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Description
Focal Adhesion Kinase (FAK) is a cytoplasmic tyrosine kinase that associates with integrins in focal adhesions. Its cellular localization is directed by a 125-amino acid sequence at the C terminus called the “Focal Adhesion Targeting” (FAT) domain, and the phosphorylation state of serine 910 (S910) in the FAT domain may regulate the assembly of focal adhesions. Furthermore, the binding of extracellular matrix ligands to integrins triggers tyrosine phosphorylations near FAK's kinase domain that increase its kinase activity, and additional tyrosine phosphorylations near proline-rich motifs create binding sites for the SH2 domains of various adaptor proteins. FAK's ability to bind numerous structural and signaling proteins via a variety of interactions regulates FAK's targeting to focal adhesions, modulates its kinase activity, and initiates intracellular signaling cascades. Thus, studies suggest that FAK may integrate cellular events controlling cell motility, growth, and invasiveness. The K73-480 monoclonal antibody recognizes the phosphorylated S910 of human FAK. The orthologous phosphorylation sites in mouse and rat FAK are S948 and S913, respectively.
Intracellular Staining
Specifications
| FAK (pS910) | |
| Monoclonal | |
| PE | |
| Mouse | |
| Affinity Purified | |
| RUO | |
| Primary | |
| Store undiluted at 4°C and protected from prolonged exposure to light. Do not freeze. |
| Flow Cytometry | |
| K73-480 | |
| Aqueous buffered solution containing BSA and ≤0.09% sodium azide. | |
| Phosphorylated Human FAK Peptide | |
| 50 Tests | |
| Cell Biology | |
| Human, Mouse, Rat | |
| IgG2b κ |
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