Key Spec Table
|Species Reactivity||Key Applications||Host||Format||Antibody Type|
|Av, H, M, R||ICC, IP||M||Purified||Monoclonal Antibody|
|Description||Anti-FAK Antibody, clone 2A7|
|Presentation||Protein G Purified immunoglobulin in Protein G Purified immunoglobulin in Purified immunoglobulin in 10mM PBS, pH 7.4 containing no preservatives.|
|Application||Anti-FAK Antibody, clone 2A7 detects level of FAK & has been published & validated for use in IC & IP.|
|Application Notes||Not recommended in Western Blot|
|Safety Information according to GHS|
|Material Size||200 µg|
|Anti-FAK, clone 2A7 (mouse monoclonal IgG1)||3084566|
|Anti-FAK, clone 2A7 (mouse monoclonal IgG1) -2444083||2444083|
|Anti-FAK, clone 2A7 - 0701050542||0701050542|
|Anti-FAK, clone 2A7 - 16028||16028|
|Anti-FAK, clone 2A7 - 16386||16386|
|Anti-FAK, clone 2A7 - 17763||17763|
|Anti-FAK, clone 2A7 - 19450||19450|
|Anti-FAK, clone 2A7 - 2070093||2070093|
|Anti-FAK, clone 2A7 - 21121||21121|
|Anti-FAK, clone 2A7 - 23166||23166|
|Reference overview||Application||Species||Pub Med ID|
|Ambivalent role of pFAK-Y397 in serous ovarian cancer--a study of the OVCAD consortium.|
Aust, S; Auer, K; Bachmayr-Heyda, A; Denkert, C; Sehouli, J; Braicu, I; Mahner, S; Lambrechts, S; Vergote, I; Grimm, C; Horvat, R; Castillo-Tong, DC; Zeillinger, R; Pils, D
Molecular cancer 13 67 2014
Focal adhesion kinase (FAK) autophosphorylation seems to be a potential therapeutic target but little is known about the role and prognostic value of FAK and pFAK in epithelial ovarian cancer (EOC). Recently, we validated a gene signature classifying EOC patients into two subclasses and revealing genes of the focal adhesion pathway as significantly deregulated.FAK expression and pFAK-Y397 abundance were elucidated by immunohistochemistry and microarray analysis in 179 serous EOC patients. In particular the prognostic value of phosphorylated FAK (pFAK-Y397) and FAK in advanced stage EOC was investigated.Multiple Cox-regression analysis showed that high pFAK abundance was associated with improved overall survival (HR 0.54; p = 0.034). FAK was positive in a total of 92.2% (n = 165) and high pFAK abundance was found in 36.9% (n = 66). High pFAK abundance (36.9% ; n = 66) was associated with either nodal positivity and/or distant metastasis (p = 0.030). Whole genome gene expression data revealed a connection of the FAK-pFAK-Y397 axis and the mTOR-S6K1 pathway, shown to play a major role in carcinogenesis.The role of pFAK-Y397 remains controversial: although high pFAK-Y397 abundance is associated with distant and lymph node metastases, it is independently associated with improved overall survival.
|FAK is required for tension-dependent organization of collective cell movements in Xenopus mesendoderm.|
Bjerke, MA; Dzamba, BJ; Wang, C; DeSimone, DW
Developmental biology 394 340-56 2014
Collective cell movements are integral to biological processes such as embryonic development and wound healing and also have a prominent role in some metastatic cancers. In migrating Xenopus mesendoderm, traction forces are generated by cells through integrin-based adhesions and tension transmitted across cadherin adhesions. This is accompanied by assembly of a mechanoresponsive cadherin adhesion complex containing keratin intermediate filaments and the catenin-family member plakoglobin. We demonstrate that focal adhesion kinase (FAK), a major component of integrin adhesion complexes, is required for normal morphogenesis at gastrulation, closure of the anterior neural tube, axial elongation and somitogenesis. Depletion of zygotically expressed FAK results in disruption of mesendoderm tissue polarity similar to that observed when expression of keratin or plakoglobin is inhibited. Both individual and collective migrations of mesendoderm cells from FAK depleted embryos are slowed, cell protrusions are disordered, and cell spreading and traction forces are decreased. Additionally, keratin filaments fail to organize at the rear of cells in the tissue and association of plakoglobin with cadherin is diminished. These findings suggest that FAK is required for the tension-dependent assembly of the cadherin adhesion complex that guides collective mesendoderm migration, perhaps by modulating the dynamic balance of substrate traction forces and cell cohesion needed to establish cell polarity.
|Development and characterization of rifampicin-resistant mutants from high virulent strains of Flavobacterium columnare.|
O Olivares-Fuster,C R Arias
Journal of fish diseases 34 2011
Flavobacterium columnare is divided into three genetic groups or genomovars, genomovar II being highly virulent for channel catfish. A modified live vaccine is currently available to prevent columnaris disease under the licensed name Aquavac-Col(®) . The strain of F. columnare used to generate the avirulent rifampicin-resistant mutant used in Aquavac-Col(®) belonged to genomovar I, the less virulent group towards channel catfish. In this study, we describe the generation and characterization of rifampicin-resistant mutants from genomovar II strains. A total of 13 new mutants were obtained, and eight of them (two from each parent strain) were genetically and phenotypically characterized. Highly conserved regions within the ribosomal operons were identical between parent and mutant strains. Genetic differences between mutants and their parent strains were revealed by amplified fragment length polymorphism (AFLP). Genetic changes were distinctive among different mutants. Analysis of the lipopolysaccharide (LPS) showed that while some mutants lacked a few molecular bands of the LPS, some exhibited the same LPS profiles as their parent strains. Comparison between immunogenic proteins from mutants and parents was carried out by immunoblot analysis and further confirmed the uniqueness of individual mutants. A complete set of rifampicin-resistant mutants with different genetic and immunogenic properties from the highly virulent genomovar II has been created. These mutants may have the potential of becoming vaccine candidates against columnaris disease.
|Receptor-interacting protein shuttles between cell death and survival signaling pathways.|
Kamarajan, P; Bunek, J; Lin, Y; Nunez, G; Kapila, YL
Molecular biology of the cell 21 481-8 2010
Cross-talk between apoptosis and survival signaling pathways is crucial for regulating tissue processes and mitigating disease. We report that anoikis-apoptosis triggered by loss of extracellular matrix contacts-activates a CD95/Fas-mediated signaling pathway regulated by receptor-interacting protein (RIP), a kinase that shuttles between CD95/Fas-mediated cell death and integrin/focal adhesion kinase (FAK)-mediated survival pathways. RIP's death domain was critical for RIP and Fas association to mediate anoikis. Fas or RIP attenuation reduced this association and suppressed anoikis, whereas their overexpression had the reverse effect. Overexpressing FAK restored RIP and FAK association and inhibited anoikis. Thus, RIP shuttles between CD95/Fas death and FAK survival signaling to mediate anoikis.Full Text Article
|Variations of proline-rich kinase Pyk2 expression correlate with prostate cancer progression.|
R Stanzione, A Picascia, P Chieffi, C Imbimbo, A Palmieri, V Mirone, S Staibano, R Franco, G De Rosa, J Schlessinger, D Tramontano
Laboratory investigation; a journal of technical methods and pathology 81 51-9 2001
Proline-rich kinase 2 (Pyk2), also known as CAKbeta (cell adhesion kinase beta), is a cytoplasmic tyrosine kinase that is structurally related to focal adhesion kinase. Pyk2 is expressed in different cell types including brain cells, fibroblasts, platelets, and other hemopoietic cells. Pyk2 is rapidly tyrosine phosphorylated in response to diverse extracellular signals acting via different post receptor pathways. We have investigated whether this protein kinase is functionally expressed in normal and neoplastic prostate tissues. In this study, we demonstrate that Pyk2 is expressed only in normal epithelial prostate tissue and in benign prostatic hyperplasia, whereas its expression progressively declines with an increasing grade of malignancy of prostate cancer.
|E-cadherin regulates anchorage-independent growth and survival in oral squamous cell carcinoma cells|
Kantak, S. S. and Kramer, R. H.
J Biol Chem, 273:16953-61 (1998) 1998
|Protein-tyrosine phosphatase alpha regulates Src family kinases and alters cell-substratum adhesion|
Harder, K. W., et al
J Biol Chem, 273:31890-900 (1998) 1998
|Immunoblotting (Western), Immunoprecipitation||9822658|
|Insulin receptor substrate-1 as a signaling molecule for focal adhesion kinase pp125(FAK) and pp60(src)|
Lebrun, P., et al
J Biol Chem, 273:32244-53 (1998) 1998
|Bombesin, vasopressin, lysophosphatidic acid, and sphingosylphosphorylcholine induce focal adhesion kinase activation in intact Swiss 3T3 cells|
Rodriguez-Fernandez, J. L. and Rozengurt, E.
J Biol Chem, 273:19321-8 (1998) 1998
|Tyrosine phosphorylation of paxillin and focal adhesion kinase during insulin-like growth factor-I-stimulated lamellipodial advance.|
Leventhal, P S, et al.
J. Biol. Chem., 272: 5214-8 (1997) 1997
In the current studies, we examined whether focal adhesion kinase (FAK) and paxillin play a role in insulin-like growth factor-I (IGF-I)-stimulated morphological changes in neuronal cells. In SH-SY5Y human neuroblastoma cells, 10 nM IGF-I enhanced the extension of lamellipodia within 30 min. Scanning electron microscopy and staining with rhodamine-phalloidin showed that these lamellipodia displayed ruffles, filopodia, and a distinct meshwork of actin filaments. Immunofluorescent staining identified focal concentrations of FAK, paxillin, and phosphotyrosine within the lamellipodia. Immunoprecipitation experiments revealed that FAK and paxillin are tyrosine-phosphorylated during IGF-I-stimulated lamellipodial extension. Maximal phosphorylation of FAK and paxillin was observed 15-30 min after the addition of 10 nM IGF-I, whereas maximal IGF-I receptor phosphorylation occurred within 5 min. FAK, paxillin, and IGF-I receptor tyrosine phosphorylation had similar concentration-response curves and were inhibited by the receptor blocking antibody alphaIR-3. These results indicate that FAK and paxillin are tyrosine-phosphorylated during IGF-I-stimulated lamellipodial advance and suggest that the tyrosine phosphorylation of these two proteins helps mediate IGF-I-stimulated cell and growth cone motility. These responses contrast directly with recent reports showing insulin-stimulated dephosphorylation of FAK and paxillin.