|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||119233 Da|
|Other Names||Focal adhesion kinase 1, FADK 1, Focal adhesion kinase-related nonkinase, FRNK, Protein phosphatase 1 regulatory subunit 71, PPP1R71, Protein-tyrosine kinase 2, p125FAK, pp125FAK, PTK2, FAK, FAK1|
|Target/Specificity||A synthetic peptide corresponding to residues in human FAK were used as an immunogen|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||FAK Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryonic development and placenta development. Required for embryonic angiogenesis, normal cardiomyocyte migration and proliferation, and normal heart development. Regulates axon growth and neuronal cell migration, axon branching and synapse formation; required for normal development of the nervous system. Plays a role in osteogenesis and differentiation of osteoblasts. Functions in integrin signal transduction, but also in signaling downstream of numerous growth factor receptors, G-protein coupled receptors (GPCR), EPHA2, netrin receptors and LDL receptors. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling cascade. Promotes localized and transient activation of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and thereby modulates the activity of Rho family GTPases. Signaling via CAS family members mediates activation of RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ACTN1, ARHGEF7, GRB7, RET and WASL. Promotes phosphorylation of PXN and STAT1; most likely PXN and STAT1 are phosphorylated by a SRC family kinase that is recruited to autophosphorylated PTK2/FAK1, rather than by PTK2/FAK1 itself. Promotes phosphorylation of BCAR1; GIT2 and SHC1; this requires both SRC and PTK2/FAK1. Promotes phosphorylation of BMX and PIK3R1. Isoform 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription.|
|Cellular Location||Cell junction, focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Note=Constituent of focal adhesions Detected at microtubules|
|Tissue Location||Detected in B and T-lymphocytes. Isoform 1 and isoform 6 are detected in lung fibroblasts (at protein level) Ubiquitous.|
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Provided below are standard protocols that you may find useful for product applications.
Focal adhesion kinase (FAK) is a non-receptor protein-tyrosine kinase implicated in signaling pathways involved in cell motility, proliferation and apoptosis (1). FAK is composed of a central catalytic domain flanked by large N- and C-terminal regions. FAK is activated by phosphorylation at tyrosine 397 in response to integrin clustering which can be induced by cell adhesion or antibody cross-linking or via G-protein-coupled receptor (GPCR) occupancy by ligands such as bombesin or lysophosphatidic acid (2-3). Phosphorylation of FAK Tyr-397 creates a binding site for Src-family kinases, and phosphorylation of FAK Tyr-576/Tyr-577 in the kinase domain activation loop enhances catalytic activity (4). Increased FAK expression has been correlated with the enhanced motility and invasiveness of human tumor cells, as well as with promoting increased cell proliferation (5).
1. Schaller, M.D. (2001) Biochim. Biophys. Acta 1540, 1
2. Schaller, M.D., et al. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 5192
3. Salazar, E.P, et al. (1999) J. Biol. Chem. 274, 28371
4. Tremblay L., et al. Int. J. Cancer, 68: 164-171, 1996
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