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抗Human PTK2B 抗体:
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抗Rat (Rattus) PTK2B 抗体:
Human Monoclonal PTK2B Primary Antibody for ICS - ABIN1177155
Anand, Cucchiarini, Terwilliger, Ganju: The tyrosine kinase Pyk2 mediates lipopolysaccharide-induced IL-8 expression in human endothelial cells. in Journal of immunology (Baltimore, Md. : 1950) 2008
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Human Monoclonal PTK2B Primary Antibody for ICS - ABIN1177156
Faure, Corvol, Toutant, Valjent, Hvalby, Jensen, El Messari, Corsi, Kadaré, Girault: Calcineurin is essential for depolarization-induced nuclear translocation and tyrosine phosphorylation of PYK2 in neurons. in Journal of cell science 2007
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Human Monoclonal PTK2B Primary Antibody for IHC, ELISA - ABIN1724705
Dylla, Deyle, Theunissen, Padurean, Verfaillie: Integrin engagement-induced inhibition of human myelopoiesis is mediated by proline-rich tyrosine kinase 2 gene products. in Experimental hematology 2004
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Human PTK2B Primary Antibody for IHC - ABIN966926
Gluck: Acid sensing in renal epithelial cells. in The Journal of clinical investigation 2004
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Human Polyclonal PTK2B Primary Antibody for IHC (p), WB - ABIN546432
Krishnan, Sharma-Walia, Streblow, Naranatt, Chandran: Focal adhesion kinase is critical for entry of Kaposi's sarcoma-associated herpesvirus into target cells. in Journal of virology 2006
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Human Polyclonal PTK2B Primary Antibody for IHC, WB - ABIN6711888
Li, Zhang, Chen, Du, Wang, Wang: Modeled microgravity causes changes in the cytoskeleton and focal adhesions, and decreases in migration in malignant human MCF-7 cells. in Protoplasma 2010
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Human Polyclonal PTK2B Primary Antibody for IHC - ABIN6714131
Cao, Chen, Fu, Qian, Ren, Su, Luo, Dai, Huang, Yan, Wu, Yan, Wang: High expression of proline-rich tyrosine kinase 2 is associated with poor survival of hepatocellular carcinoma via regulating phosphatidylinositol 3-kinase/AKT pathway. in Annals of surgical oncology 2014
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Human Polyclonal PTK2B Primary Antibody for IF (p), IHC (p) - ABIN745763
Cao, Zheng, Wang, Wang, Li, Li, Lai, Wang, Qin: Src blockage by siRNA inhibits VEGF-induced vascular hyperpemeability and osteoclast activity - an in vitro mechanism study for preventing destructive repair of osteonecrosis. in Bone 2015
LFA-1 cross-linking recruits and activates FAK1 and PYK2 to phosphorylate LAT selectively on a single Y-171 site that binds to the GRB2-SKAP1 complex and limits dwell times of T-cells with dendritic cells
Pyk2 has a role in spine structure and synaptic function; its deficit contributes to Huntington's disease cognitive impairments
Results provide evidence that Pyk2 phosphorylates STIM1 at its Y361 residue, activating thereby store-operated Ca(2+) entry.
The authors' findings identify Pyk2 as a unique mediator of invadopodium formation and function and also provide a novel insight into the mechanisms by which Pyk2 mediates tumor cell invasion.
Results show that VEGFA induces Pyk2 activation in mediating human retinal microvascular endothelial cell migration, sprouting and tube formation, and that Pyk2-mediated STAT3 activation is required for hypoxia-induced retinal neovascularization.
Interestingly, rs2279590 locus has a widespread enhancer effect on two nearby genes, protein tyrosine kinase 2 beta (PTK2B) and epoxide hydrolase-2 (EPHX2); both of which have been previously associated with AD as risk factors.
thrombin binding to PAR-1 receptor activated Gi-protein/c-Src/Pyk2/EGFR/PI3K/Akt/p42/p44 MAPK cascade, which in turn elicited AP-1 activation and ultimately evoked MMP-9 expression and cell migration in SK-N-SH cells.
Multiple myeloma that is driven by deregulated iron homeostasis and/or Pyk2/beta-cateninn signaling is susceptible to deferasirox-induced apoptosis.
In summary, our data suggested that PYK2 via S6K1 activation modulated AR function and growth properties in prostate cancer cells. Thus, PYK2 and S6K1 may potentially serve as therapeutic targets for PCa treatment.
Our findings suggest that Pyk2 plays an important role in the coordination of stabilization of beta-catenin in the crosstalk between Wnt/beta-catenin and Wnt/Ca(2+) signaling pathways upon Wnt3a stimulation in differentiating hNPCs.
STIM1-induced Ca(2+) signaling activates Pyk2 to inhibit the interaction of VE-PTP and VE-cadherin and hence increase endothelial permeability.
Ascites and CCL18 stimulate the phosphorylation and expression of Pyk2, which positively regulates ascites-induced ovarian cancer cell migration.
We demonstrated trophoblast cytoprotection by intervention with supraphysiological concentrations of relaxin, a process in part mediated through the PI3-kinase-Akt/PKB cell survival pathway. These results provide further rationale for clinical investigation of relaxin as a potential therapeutic in preeclampsia.
PTK2B polymorphism (rs28834970) could modify the risk of late-onset Alzheimer's disease (LOAD), and PTK2B polymorphism (rs28834970) and APOE may interact to increase LOAD risk in a Han Chinese population.
Studies suggest that PYK2 is a common downstream effector of ErbB and IL8 receptors, and that PYK2 integrates their signaling pathways through a positive feedback loop to potentiate breast cancer invasion.
Pyk2 is a key downstream signaling molecules of CCR7 in SCCHN, which promotes SCCHN tumorigenesis and progression.
Phosphoproteomic analysis identifies FAK2 as a potential therapeutic target for tamoxifen resistance in breast cancer.
Pyk2-focal adhesion targeting domain interacts with and binds to leupaxin.
Src has a role in priming Pyk2 (but not FAK) phosphorylation and subsequent activation downstream of integrins
Data strongly suggest that chemokine-stimulated associations between Vav1, SLP-76, and ADAP facilitate Rac1 activation and alpha4beta1-mediated adhesion, whereas Pyk2 opposes this adhesion by limiting Rac1 activation.
In the absence of Pky2 there is a slight decrease in plaque formation in cortex and hippocampus and an increase in plaque formation following Pky2 over-expression.
the non-receptor protein tyrosine kinase 2 beta (PTK2B) plays a critical role in murine beige adipocyte differentiation.
Data provide evidence that activated PYK2 may function as a component of the microtubule organizing center to regulate spindle assembly during the meiotic process of mouse oocytes.
MMP-9 activation by hypoxia requires LRP1 and Pyk2 phosphorylation in fibroblasts.
results suggest that although Pyk2 and FAK are involved in inflammasome activation, only Pyk2 directly phosphorylates ASC and brings ASC into an oligomerization-competent state by allowing Tyr146 phosphorylation to participate ASC speck formation and subsequent NLRP3 inflammation.
Osteoprotegerin may induce podosome reassembly and peripheral adhesive structure detachment by modulating phosphorylation of Pyk2 and Src and their intracellular distribution in osteoclasts.
These results suggest that mechanical stimuli activate P2X7 might induce ECMPs expression through PYK2 except in the case of OPN expression. Altogether, mechanical stimuli-induced ECMPs production might be implicated by extracellular ATP secretion or integrin via PYK2 activation.
Lineage-tracing of monocyte populations suggests that Pyk2 promotes apoptosis in BM monocytes, thereby acting as an important homeostatic regulator of turnover in these short-lived, innate immune cells.
Pyk2 selectively contributes to the coordination of phagocytosis-promoting signals downstream of CR3, but is dispensable for FcgammaR-mediated phagocytosis
the findings suggest a model in which the oocyte is not a passive participant in fertilization, but instead responds to sperm contact by localized PYK2 signaling that promotes actin remodeling events required to physically incorporate the sperm head into the ooplasm.
results show that Pyk2 contributes to cytotoxic T lymphocyte(CTL) migration by regulating detachment of CTL at the trailing edge, which could explain why Pyk2 is important for chemotactic and migratory responses.
Defects in Pyk2 suppress Kawasaki Disease-like experimental vasculitis, presumably through CXCL9- and CXCL10-dependent interference with neo-angiogenesis. Since Pyk2-KO mice show no life-threatening phenotype, Pyk2 may be a promising therapeutic molecular target for KD.
At fertilization, Pyk2 and p-Pyk2 were detected predominantly in sperm heads and the oocyte cytoplasm. Upon formation of male and female pronuclei, Pyk2 and its activated form accumulate in the two pronuclei. Pyk2 was in blastomere nuclei and the pre-blastula cytoplasm. Pyk2 and its activated form then localized to the perinuclear regions, where blastula cells come into contact with each other.
Findings indicate the presence of unique and overlapping Pyk2 signaling pathways in osteoblasts, which may be controlled by regulating the phosphorylation, kinase activity, and scaffolding functions of Pyk2.
Astrocytes from Pyk2-/- mice displayed a slower wound covering as compared with wild-type littermate mice after a mechanical stab lesion, data confirmed in purified astrocytes in vitro; actin polymerization dynamics was altered in Pyk2-/- astrocytes; gelsolin, an actin-capping protein able to interact with Pyk2, was mislocalized in Pyk2-/- migrating astrocytes compared with Pyk2+/+ astrocytes
Resistance to hypoxia-induced PH was markedly higher in Pyk2-deficient mice than in wild-type mice. Pyk2-dependent generation of ROS is necessary for the activation of HIF-1alpha.
Ptk2b activation may play a key role in the signaling responses in ECs under hemodynamic influence [proline-rich tyrosine kinase 2]
This gene encodes a cytoplasmic protein tyrosine kinase which is involved in calcium-induced regulation of ion channels and activation of the map kinase signaling pathway. The encoded protein may represent an important signaling intermediate between neuropeptide-activated receptors or neurotransmitters that increase calcium flux and the downstream signals that regulate neuronal activity. The encoded protein undergoes rapid tyrosine phosphorylation and activation in response to increases in the intracellular calcium concentration, nicotinic acetylcholine receptor activation, membrane depolarization, or protein kinase C activation. This protein has been shown to bind CRK-associated substrate, nephrocystin, GTPase regulator associated with FAK, and the SH2 domain of GRB2. The encoded protein is a member of the FAK subfamily of protein tyrosine kinases but lacks significant sequence similarity to kinases from other subfamilies. Four transcript variants encoding two different isoforms have been found for this gene.
, FADK 2
, PTK2B protein tyrosine kinase 2 beta
, calcium-dependent tyrosine kinase
, calcium-regulated non-receptor proline-rich tyrosine kinase
, cell adhesion kinase beta
, focal adhesion kinase 2
, proline-rich tyrosine kinase 2
, protein kinase B
, protein-tyrosine kinase 2-beta
, related adhesion focal tyrosine kinase
, cellular adhesion kinase beta
, protein tyrosine kinase 2 beta
, CAK beta
, PTK2 protein tyrosine kinase 2 beta
, protein tyrosine kinase 2.2
, protein tyrosine kinase 2aa
, protein tyrosine kinase 2b