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Results show that VEGFA (zeige VEGFA Proteine) induces Pyk2 activation in mediating human retinal microvascular endothelial cell migration, sprouting and tube formation, and that Pyk2-mediated STAT3 (zeige STAT3 Proteine) 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 (zeige EPHX2 Proteine)); both of which have been previously associated with AD as risk factors.
thrombin (zeige F2 Proteine) binding to PAR-1 (zeige MARK2 Proteine) receptor activated Gi-protein/c (zeige PROC Proteine)-Src (zeige SRC Proteine)/Pyk2/EGFR (zeige EGFR Proteine)/PI3K (zeige PIK3CA Proteine)/Akt (zeige AKT1 Proteine)/p42/p44 (zeige PSMC6 Proteine) MAPK (zeige MAPK3 Proteine) cascade, which in turn elicited AP-1 (zeige FOSB Proteine) activation and ultimately evoked MMP-9 (zeige MMP9 Proteine) 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 (zeige RPS6KB1 Proteine) activation modulated AR function and growth properties in prostate cancer cells. Thus, PYK2 and S6K1 (zeige RPS6KB1 Proteine) may potentially serve as therapeutic targets for PCa (zeige FLVCR1 Proteine) treatment.
Our findings suggest that Pyk2 plays an important role in the coordination of stabilization of beta-catenin (zeige CTNNB1 Proteine) in the crosstalk between Wnt (zeige WNT2 Proteine)/beta-catenin (zeige CTNNB1 Proteine) and Wnt (zeige WNT2 Proteine)/Ca(2 (zeige CA2 Proteine)+) signaling pathways upon Wnt3a (zeige WNT3A Proteine) stimulation in differentiating hNPCs.
STIM1 (zeige STIM1 Proteine)-induced Ca(2 (zeige CA2 Proteine)+) signaling activates Pyk2 to inhibit the interaction of VE-PTP (zeige PTPRB Proteine) and VE-cadherin (zeige CDH5 Proteine) and hence increase endothelial permeability.
Ascites and CCL18 (zeige CCL18 Proteine) 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 (zeige PIK3CA Proteine)-Akt/PKB (zeige AKT1 Proteine) 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.
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 (zeige MMP9 Proteine) activation by hypoxia requires LRP1 (zeige LRP1 Proteine) and Pyk2 phosphorylation in fibroblasts.
results suggest that although Pyk2 and FAK (zeige PTK2 Proteine) are involved in inflammasome activation, only Pyk2 directly phosphorylates ASC (zeige STS Proteine) and brings ASC (zeige STS Proteine) into an oligomerization-competent state by allowing Tyr146 phosphorylation to participate ASC (zeige STS Proteine) speck formation and subsequent NLRP3 (zeige NLRP3 Proteine) inflammation.
Osteoprotegerin (zeige TNFRSF11B Proteine) may induce podosome reassembly and peripheral adhesive structure detachment by modulating phosphorylation of Pyk2 and Src (zeige SRC Proteine) and their intracellular distribution in osteoclasts.
These results suggest that mechanical stimuli activate P2X7 (zeige P2RX7 Proteine) might induce ECMPs expression through PYK2 except in the case of OPN (zeige SPP1 Proteine) 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 (zeige ITGAM Proteine), 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 (zeige CXCL9 Proteine)- and CXCL10 (zeige CXCL10 Proteine)-dependent interference with neo-angiogenesis. Since Pyk2-KO mice show no life-threatening phenotype, Pyk2 may be a promising therapeutic molecular target for KD.
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