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PTK2 encodes a cytoplasmic protein tyrosine kinase which is found concentrated in the focal adhesions that form between cells growing in the presence of extracellular matrix constituents. Additionally we are shipping FAK Kits (28) and FAK Proteins (12) and many more products for this protein.
Showing 10 out of 652 products:
Chicken Monoclonal FAK Primary Antibody for BI, IP - ABIN967736
Clancy, Rediske, Tang, Nijher, Frenkel, Philips, Abramson: Outside-in signaling in the chondrocyte. Nitric oxide disrupts fibronectin-induced assembly of a subplasmalemmal actin/rho A/focal adhesion kinase signaling complex. in The Journal of clinical investigation 1997
Show all 7 references for ABIN967736
Human Polyclonal FAK Primary Antibody for EIA, WB - ABIN453801
Calalb, Polte, Hanks: Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases. in Molecular and cellular biology 1995
Show all 3 references for ABIN453801
Human Polyclonal FAK Primary Antibody for IF, IHC - ABIN1532612
Olsen, Blagoev, Gnad, Macek, Kumar, Mortensen, Mann: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. in Cell 2006
Human Polyclonal FAK Primary Antibody for FACS, IF - ABIN652554
Ma, He, Zhang, Fei, Niu, Wang, Ding, Xu, Chen, Zhu: DNA methylation-regulated miR-193a-3p dictates resistance of hepatocellular carcinoma to 5-fluorouracil via repression of SRSF2 expression. in The Journal of biological chemistry 2012
Human Polyclonal FAK Primary Antibody for IHC, ELISA - ABIN1533050
Lee, Strunk, Spritz: A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes. in Oncogene 1993
In human colon cancer cells, Akt1 (show AKT1 Antibodies) binds focal adhesion kinase via the Akt1 kinase (show AKT1 Antibodies) domain independently of the pleckstrin (show PLEK Antibodies) homology domain
FAK enhances glycolysis and decreases mitochondrial respiration and increases key glycolytic proteins. Active/tyrosine-phosphorylated FAK directly binds to PKM2 and promotes PKM2-mediated glycolysis.
Our findings suggest that the targets of FAK play a key role in metastasis
Data suggest that, in colonic/prostatic neoplasm cells, increased expression of NDRG1 decreases activating phosphorylation of FAK and paxillin; silencing/inhibition of NDRG1 results in opposite effect and inhibits neoplasm cell migration/adhesion.
Collectively, our data demonstrate that DCMF induces cell migration and promotes wound healing through activation of Src (show SRC Antibodies)/FAK, ERK (show EPHB2 Antibodies), AKT (show AKT1 Antibodies), and p38 MAPK (show MAPK14 Antibodies) signaling.
These results suggest that ITCs could be potential agents for the prevention of C6 glioma cell migration and invasion by decreasing FAK/JNK (show MAPK8 Antibodies)-mediated MMP-9 (show MMP9 Antibodies) expression
In clinical samples of hepatocellular carcinom (HCC (show FAM126A Antibodies)), miR (show MLXIP Antibodies)-379-5p negatively correlated with FAK, which was up-regulated in HCC (show FAM126A Antibodies).
Combining erlotinib with FAK inhibitor was also potent in vivo as evidenced by reduced tumor growth in the A549 mouse xenograft model.
Increased focal adhesion kinase(FAK)activity.
Results from immunohistochemical analyses in 9 benign, 19 premalignant, and 19 malignant oral tissues showed that the immunoreactivity of FAK was observed in 5 benign (56%), 19 premalignant (100%), and 18 malignant tissues (95%)
FAK is required for external force-induced spindle reorientation, suggesting that FAK's involvement in this process stems from a role in the transduction of external forces to the cell cortex.
FAK is required for tension-dependent organization of collective cell movements in Xenopus mesendoderm.
work identifies new roles for the FERM domain in the regulation of the dynamics of FAK on its signaling complexes in vivo and in vitro and identifies epiboly as the earliest developmental process in which FAK plays a crucial role during development
These data suggest an important role for the FERM domain in the activation of FAK.
FAK phosphorylation at Y861 is essential for lamellipodial protrusion induced by BDNF (show BDNF Antibodies), while phosphorylation at Y925 controls the rate of point contact turnover.
Data imply that FAK plays an essential role in chamber outgrowth and looping morphogenesis.
FAK is required for proper topographic positioning of retinal axons along the anterior-posterior axis of the optic tectum in Xenopus and zebrafish, a guidance decision mediated in part by A-type ephrins.
results suggest that LPS (show TLR4 Antibodies)-stimulated macrophage mediators attenuate both FAK and Src (show SRC Antibodies) activations in osteoblast, suggesting a novel role for TNFalpha (show TNF Antibodies) on osteoblast performance
Report phosphorylation sites in focal adhesion kinase and putative new binding partners.
data indicate that PTPalpha (show PTPRA Antibodies) and FAK, which are enriched in FAs (show FAS Antibodies), interact with IP3R1 (show ITPR1 Antibodies) at adjacent ER sites to spatially sequester IL-1 (show IL1A Antibodies)-induced Ca(2 (show CA2 Antibodies)+) signalling
FAK-regulated signalling module PDK1 (show PDPK1 Antibodies)-Akt (show AKT1 Antibodies)-p70S6K (show RPS6KB1 Antibodies) that controls Src's intracellular trafficking operates at Src (show SRC Antibodies)-containing autophagosomes.
Data show that active active focal adhesion kinase (FAK) localizes to integrin-containing endosomes.
FAK deletion correlates with increased phosphorylation of Tks-5 (show SH3PXD2A Antibodies) (tyrosine kinase substrate (show IRS2 Antibodies) with five SH3 domain (show ITSN1 Antibodies)) and reactive oxygen species production.
Par4 (show F2RL3 Antibodies), CEBPB (show CEBPB Antibodies) and FAK form a senescence signaling pathway, playing roles in modulating cell survival, growth, apoptosis, EMT (show ITK Antibodies) and self-renewal
LPS (show TLR4 Antibodies)-induced increases in intestinal TJP and intestinal inflammation were regulated by TLR4 (show TLR4 Antibodies)-dependent activation of the FAK/MyD88 (show MYD88 Antibodies)/IL-1R-associated kinase 4 signaling pathway.
Inactivation of the FAK signaling pathway by either genetic or pharmacologic methods significantly sensitizes both murine and human PTEN (show PTEN Antibodies)-null T-ALL cells to PI3K/AKT (show AKT1 Antibodies)/mTOR (show FRAP1 Antibodies) inhibition when cultured in vitro on feeder layer cells or a matrix and in vivo
These data indicate that FAK might exaggerate NMDAR (show GRIN1 Antibodies)-mediated synaptic transmission in the spinal dorsal horn to sensitize nociceptive behaviors.
RhoA (show RHOA Antibodies) and membrane fluidity mediates the spatially polarized Src (show SRC Antibodies)/FAK activation in response to shear stress.
XIAP (show XIAP Antibodies) plays an essential role in shear stress-stimulated FAK phosphorylation.
mitochondrial oxidants generated in response to endothelial strain trigger FAK phosphorylation through a signaling pathway that involves protein kinase C (show PKC Antibodies)
These results suggest that TGF-beta1 (show TGFB1 Antibodies)-induced monolayer permeability involves focal adhesion and cytoskeletal rearrangement through both FAK/Src (show SRC Antibodies)-dependent and -independent pathways.
Results suggest focal adhesion kinase is involved in thrombospondin-1 (show THBS1 Antibodies)-induced vascular smooth muscle cell migration.
This gene encodes a cytoplasmic protein tyrosine kinase which is found concentrated in the focal adhesions that form between cells growing in the presence of extracellular matrix constituents. The encoded protein is a member of the FAK subfamily of protein tyrosine kinases but lacks significant sequence similarity to kinases from other subfamilies. Activation of this gene may be an important early step in cell growth and intracellular signal transduction pathways triggered in response to certain neural peptides or to cell interactions with the extracellular matrix. Several transcript variants encoding different isoforms have been found for this gene, but the full-length natures of only three of them have been determined.
, FAK-related non-kinase polypeptide
, PTK2 protein tyrosine kinase 2
, focal adhesion kinase 1
, focal adhesion kinase-related nonkinase
, protein phosphatase 1 regulatory subunit 71
, protein phosphatase 1, regulatory subunit 71
, protein-tyrosine kinase 2
, focal adhesion kinase pp125FAK
, focal ashension kinase 1
, focal adhesion kinase