Focal Adhesion Kinase
Focal adhesion kinase (FAK), a non-receptor tyrosine kinase, is the first intracellular step in the signal transduction cascade initiated by the attachment of an integrin to the extracellular matrix at points known as focal adhesions. FAK has a key role in cellular migration and motility.
Focal Adhesion Kinase Inhibitors |
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|---|---|
| Cat. No. | Product Name / Activity |
| 7305 | Defactinib |
| Potent and selective FAK and Pyk2 inhibitor | |
| 3414 | FAK Inhibitor 14 |
| Selective FAK inhibitor | |
| 7786 | GSK 2256098 |
| Potent focal adhesion kinase (FAK) inhibitor | |
| 4278 | PF 431396 |
| Dual FAK/PYK2 inhibitor | |
| 3239 | PF 573228 |
| Potent and selective FAK inhibitor | |
| 6891 | PND 1186 |
| Potent FAK inhibitor; orally bioavailable | |
Degraders |
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| Cat. No. | Product Name / Activity |
| 7306 | FC 11 |
| Highly potent focal adhesion kinase (FAK) Degrader | |
| 7818 | GSK 215 |
| Potent and selective focal adhesion kinase (FAK) PROTAC® Degrader | |
Focal adhesion kinase (FAK), a non-receptor tyrosine kinase, is the first intracellular step in the signal transduction cascade initiated by the attachment of an integrin to the extracellular matrix at points known as focal adhesions. Therefore, FAK plays a key role in cellular migration and motility.
FAK has 3 functional domains: a focal adhesion targeting domain (FAT), a catalytic domain and a FERM domain, which mediates interactions with the cytoplasmic domains of integrins and growth factor receptors. FAK has multiple phosphorylation sites that are required for binding to adaptor proteins containing SH2 domains (e.g. Src and SH3 domains (e.g. CAS, GRAF)). Key amongst these phosphorylation sites is Tyr397, which is important for the interaction of FAK with downstream signaling molecules such as PI 3-K, PLCγ and Rho kinase.
Overexpression of FAK has been associated with several types of cancer.