SpecificityPhosphorylation site-specific antibody (PSSA) selective for the phosphorylated form of the Focal Adhesion Kinase enzyme containing a phosphate on serine 910. The antibody has been shown to recognize FAK (approximately 125 kDa) in human epithelial carcinoma cells.
Human Predicted to work with:
Mouse, Rat, Chicken, Xenopus laevis
Synthetic peptide derived from the region of FAK that contains serine 910. The sequence is conserved in human, mouse, rat, chicken and frog.
FAK is a non-receptor protein tyrosine kinase discovered as a substrate for Src and it is a key protein in integrin, growth factor and bioactive peptide signaling. 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 regulation includes phosphorylation at multiple tyrosine and serine residues. Phosphorylation of tyrosine generally is associated with positive regulation and growth promotion, however, dephosphorylation at these sites occurs as cells enter mitosis (M-Phase of the cell cycle). In contrast, serine phosphorylation either remains high or is increased as cells enter mitosis and may play a role in focal adhesion disassembly.
Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
Storage bufferPreservative: 0.05% Sodium Azide
Constituents: 50% Glycerol, Dulbecco's phosphate buffered saline (without Mg2+ and Ca2+), 1mg/ml BSA(IgG, protease free) as a carrier. pH 7.3
Concentration information loading...
PurityImmunogen affinity purified
Purification notesPurified from rabbit serum by sequential epitope-specific chromatography. The antibody has been negatively preadsorbed using (i) a non-phosphopeptide corresponding to the site of phosphorylation to remove antibody that is reactive with non-phosphorylated Focal Adhesion Kinase enzyme and (ii) a generic serine phosphorylated peptide to remove antibody that is reactive with phospho-serine, irrespective of the sequence. The final product is generated by affinity chromatography using a Focal Adhesion Kinase-derived peptide that is phosphorylated at serine 910.
Primary antibody notesFAK is a non-receptor protein tyrosine kinase discovered as a substrate for Src and it is a key protein in integrin, growth factor and bioactive peptide signaling. 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 regulation includes phosphorylation at multiple tyrosine and serine residues. Phosphorylation of tyrosine generally is associated with positive regulation and growth promotion, however, dephosphorylation at these sites occurs as cells enter mitosis (M-Phase of the cell cycle). In contrast, serine phosphorylation either remains high or is increased as cells enter mitosis and may play a role in focal adhesion disassembly.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
1/1000. Predicted molecular weight: 125 kDa.
FunctionNon-receptor protein-tyrosine kinase implicated in signaling pathways involved in cell motility, proliferation and apoptosis. Activated by tyrosine-phosphorylation in response to either integrin clustering induced by cell adhesion or antibody cross-linking, or via G-protein coupled receptor (GPCR) occupancy by ligands such as bombesin or lysophosphatidic acid, or via LDL receptor occupancy. Microtubule-induced dephosphorylation at Tyr-397 is crucial for the induction of focal adhesion disassembly. Plays a potential role in oncogenic transformations resulting in increased kinase activity.
Tissue specificityExpressed in all organs tested, in lymphoid cell lines, but most abundantly in brain.
Sequence similaritiesBelongs to the protein kinase superfamily. Tyr protein kinase family. FAK subfamily. Contains 1 FERM domain. Contains 1 protein kinase domain.
DomainThe first Pro-rich domain interacts with the SH3 domain of CRK-associated substrate (BCAR1) and CASL. The carboxy-terminal region is the site of focal adhesion targeting (FAT) sequence which mediates the localization of FAK1 to focal adhesions.
Post-translational modificationsPhosphorylated on 6 tyrosine residues upon activation. Microtubule-induced dephosphorylation at Tyr-397 could be catalyzed by PTPN11 and regulated by ZFYVE21. Dephosphorylated by PTPN11 upon EPHA2 activation by its ligand EFNA1.
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Anti-FAK (phospho S910) antibody images
Western blot - FAK (phospho S910) antibody (ab4794)
Predicted band size : 125 kDa
Specificity for detecting FAK pS910 phosphorylation using a phospho-specific antibody (PSSA): Cell extracts prepared from mitotic human epithelial carcinoma cells expressing FAK were resolved by SDS-PAGE on a 10% Tris-glycine gel, and transferred to nitrocellulose. Membranes were incubated with 0.5 µg/mL ab4794, following prior incubation in the presence of the peptide immunogen (lane 1), a generic phosphoserine peptide (lane 2), the non-phosphopeptide corresponding to the FAK phosphopeptide (lane 3), or the absence of the peptide immunogen (lane 4). After washing, membranes were incubated with goat F(ab’)2 anti-rabbit IgG alkaline phosphatase and bands were detected using the Tropix WesternStar detection method. The data show that only the phosphopeptide corresponding to the peptide immunogen blocks the antibody signal, thereby demonstrating the specificity of the ab4794 PSSA for the targeted phosphorylation site.
References for Anti-FAK (phospho S910) antibody (ab4794)
This product has been referenced in:
Wang YT et al. An informatics-assisted label-free quantitation strategy that depicts phosphoproteomic profiles in lung cancer cell invasion. J Proteome Res9:5582-97 (2010).
Read more (PubMed: 20815410) »