Product nameAnti-FAK (phospho Y925) antibody
See all FAK primary antibodies
DescriptionRabbit polyclonal to FAK (phospho Y925)
SpecificityThis antibody is specific for FAK only when phosphorylated at tyrosine 925.
Tested applicationsSuitable for: WB, ELISA, ICC/IFmore details
Species reactivityReacts with: Mouse, Rat, Human
Synthetic phosphopeptide derived from Human FAK around the phosphorylation site of tyrosine 925 (KVYpEN).
- HepG2 and 293 cell extract.
Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
Storage bufferpH: 7.40
Preservative: 0.02% Sodium azide
Constituents: 50% Glycerol, 0.87% Sodium chloride, PBS
Concentration information loading...
PurityImmunogen affinity purified
Purification notesThe antibody was affinity purified from rabbit antiserum by affinity chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation site.
Our Abpromise guarantee covers the use of ab38512 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||1/500 - 1/1000. Detects a band of approximately 123 kDa (predicted molecular weight: 119 kDa).|
|ICC/IF||Use at an assay dependent concentration. PubMed: 22102809|
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.
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.
Cellular localizationCell junction > focal adhesion. Cell membrane. Constituent of focal adhesions.
- Information by UniProt
- FADK 1 antibody
- FADK antibody
- FAK related non kinase polypeptide antibody
All lanes : Anti-FAK (phospho Y925) antibody (ab38512) at 1/500 dilution
Lane 1 : HepG2 cell lysate, pre-incubated with phosphopeptide.
Lane 2 : HepG2 cell lysate.
Lane 3 : 293 cell lysate + EGF + serum.
Lysates/proteins at 30 µg per lane.
All lanes : Alkaline Phosphatase AffiniPure Goat Anti-Rabbit IgG (H+L).
Predicted band size: 119 kDa
Observed band size: 123 kDa why is the actual band size different from the predicted?
Lanes can be loaded with 5-30µg of total protein.
ab38512 staining FAK (phospho Y925) in murine bone marrow-derived dendritic cells by Immunocytochemistry/ Immunofluorescence.
Cells were fixed with formaldehyde and blocked with 3% BSA before being incubated with primary antibody. An AlexaFluor®568-conjugated goat anti-rabbit polyclonal IgG was used as the secondary antibody.
This product has been referenced in:
- Cui S et al. Genistein inhibits the growth and regulates the migration and invasion abilities of melanoma cells via the FAK/paxillin and MAPK pathways. Oncotarget 8:21674-21691 (2017). Read more (PubMed: 28423510) »
- Gill MB et al. KSHV-TK is a tyrosine kinase that disrupts focal adhesions and induces Rho-mediated cell contraction. EMBO J 34:448-65 (2015). Read more (PubMed: 25471072) »