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抗Human PAK2 抗体:
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Cow (Bovine) Polyclonal PAK2 Primary Antibody for WB - ABIN550200
Jakobi, Huang, Walter, Tuazon, Traugh: Substrates enhance autophosphorylation and activation of p21-activated protein kinase gamma-PAK in the absence of activation loop phosphorylation. in European journal of biochemistry / FEBS 2000
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Human Monoclonal PAK2 Primary Antibody for ICC, IHC - ABIN969338
Chu, Wu, Liao, Pardo, Zhao, Li, Mendenhall, Pali, Shen, Yu, Taylor, Aversa, Molineaux, Payan, Masuda: A novel role for p21-activated protein kinase 2 in T cell activation. in Journal of immunology (Baltimore, Md. : 1950) 2004
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Human Polyclonal PAK2 Primary Antibody for IHC (p), WB - ABIN2476049
Rudel, Bokoch: Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2. in Science (New York, N.Y.) 1997
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Human Polyclonal PAK2 Primary Antibody for IHC (p), WB - ABIN541551
Jaffer, Chernoff: p21-activated kinases: three more join the Pak. in The international journal of biochemistry & cell biology 2002
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Human Polyclonal PAK2 Primary Antibody for IHC (p), WB - ABIN541550
Vilas, Corvi, Plummer, Seime, Lambkin, Berthiaume: Posttranslational myristoylation of caspase-activated p21-activated protein kinase 2 (PAK2) potentiates late apoptotic events. in Proceedings of the National Academy of Sciences of the United States of America 2006
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Human Polyclonal PAK2 Primary Antibody for IP, WB - ABIN253074
Qu, Misaghi, Izrael-Tomasevic, Newton, Gilmour, Lamkanfi, Louie, Kayagaki, Liu, Kömüves, Cupp, Arnott, Monack, Dixit: Phosphorylation of NLRC4 is critical for inflammasome activation. in Nature 2012
Knockdown of PKM2 decreased PAK2 protein half-life by increasing ubiquitin-dependent proteasomal degradation. PKM2 is overexpressed in pancreatic ductal adenocarcinoma and promotes invasion and metastasis through phosphorylation and stabilization of PAK2.
Overexpression of PAK2 in oral squamous cell carcinomas may be associated with an advanced pathology grade.
the promotion of apoptosis by human cytomegalovirusmiRUS45p in cells was specifically mediated via inhibition of PAK2 expression.
leukaemic cells explicitly require PAK2 to grow towards an extracellular matrix. PAK2-deficient cells fail to form colonies in methylcellulose and to induce lymphomas in vivo. PAK2 might therefore be the critical isoform in leukaemic cells by controlling tumour growth
Results show that PAK2 kinase plays an alternative anti-apoptotic role, phosphorylating caspase-7 and promoting unfettered cell growth and chemotherapeutic resistance.
We found that overexpression of miR-137 inhibited the proliferation of melanoma cells, which could be phenocopied by knockdown of PAK2 using siRNAs.
PAK2 is a direct effector of TSC1-TSC2-RHEB signaling and a new target for rational drug therapy in TSC.
Nef exploits PAK2 in a stepwise mechanism in which its kinase activity cooperates with an adaptor function for the exocyst complex to inhibit host cell actin dynamics.
Cytoplasmic Pak2 may promote cell proliferation in normal endometrium during menstrual cycle.
Further analyses show that HDAC6 may promote growth of GBM cells through inhibition of SMAD2 phosphorylation to downregulate p21
Pak1 and Pak2 counteract centrosome separation in a kinase-dependent manner.
Findings indicate that repression of microRNA miR-134 and consequent up-regulation of p21-activated kinase 2 (Pak2) might contribute to paclitaxel resistance.
Inhibition of PAK activation at late G2-phase centrosomes caused by Rac1 inactivation coincides with impeded activation of Aurora A and the CyclinB/Cdk1 complex and delayed mitotic entry.
Data show that group I p21-activated kinases (Paks) Pak1 and Pak2 were much more abundant than Pak3 in meningioma.
Results identified Pak2 as a possibly important mediator of ovarian cancer cell migration on extracellular matrix.
PAK2 activation may be associated with advanced tumor progression and poor prognosis of gastric cancer
Prostasin repress cancer cells and contribute to chemoresistance by modulating the CASP/PAK2-p34/actin pathway.
Authors demonstrate that HIV-1 Nef expression mediates phosphorylation of Mek1 on serine298 and Pak2 on serine192/197 in T cell lines as well as primary human T cells.
thrombin induces monocyte/macrophage migration via PAR1-Galpha12-dependent Pyk2-mediated Gab1 and p115 RhoGEF interactions, leading to Rac1- and RhoA-targeted Pak2 activation.
Cytokine-induced migration correlated with phosphorylation of PAK1 in primary myeloma cells & cell lines. Downregulation of PAK1 with siRNA in INA-6 cells resulted in decreased cytokine-driven migration.
PAK2 acts as a Rac1-dependent negative regulator of neuronal glucose uptake and insulin sensitivity.
These results identify Pak1 and Pak2 as redundant regulators of myoblast differentiation in vitro and in vivo and as components of the promyogenic Ncad/Cdo/Cdc42 signaling pathway.
PAK-mediated phosphorylation of PKD1 at Ser203 triggers its membrane dissociation and subsequent entry into the nucleus, thereby regulating the phosphorylation of PKD1 nuclear targets, including class IIa histone deacetylases.
Data indicate that resveratrol treatment inhibits neuronal glucose uptake via P21-activated kinase 2 (PAK2).
Mechanistic insights into the role of Pak2 in hematopoietic stem cells migration and homing.
Pak2 disruption decreased the survival and proliferation of multicytokine stimulated immature progenitors.
The data suggest that Pak2 controls thymic Natural Killer T-cell development by providing a signal that links Egr2 to induce PLZF, in part by regulating signaling lymphocyte activation molecule 6 expression.
In adult endothelial cells, Pak2 depletion leads to severe apoptosis and acute angiogenesis defects, and in adult mice, endothelial Pak2 deletion leads to increased vascular permeability.
Pak2 Links TCR Signaling Strength to the Development of Regulatory T Cells and Maintains Peripheral Tolerance
Failure to induce proper actin cytoskeletal remodeling impaired PLCgamma1 and Erk1/2 signaling in the absence of Pak2, uncovering the critical function of Pak2 as an essential regulator that governs the actin cytoskeleton-dependent signaling
p21-activated kinase is essential for hematopoietic stem/progenitor cell migration and engraftment.
Pak2, but not Pak1, negatively regulates RhoA via phosphorylation of the guanine nucleotide exchange factor GEF-H1 at an inhibitory site, leading to increased GEF-H1 microtubule binding and loss of RhoA stimulation
Full-length PAK-2 rather than the caspase-activated PAK-2p34 is required for normal embryonic development.
phosphorylation of merlin at serine 518 is induced by the p21-activated kinase PAK2
Caspase-activated PAK-2 is regulated by subcellular targeting and proteasomal degradation
Pak2 has a role in the down-regulation of translation initiation in apoptosis by phosphorylation of Mnk1
Rac1 and PAK2 activation that eventually controls the chemotactic response is regulated by Gi and PI3KGamma
Nef can activate murine PAK2 and associate with a small fraction of it, and may be required to induce a multiorgan AIDS-like disease in Tg mice
c-Abl represents a target downstream of phosphatidylinositol 3-kinase-activated PAK2, which differentiates TGF-beta signaling in fibroblasts and epithelial cell lines.
EphrinB ligands B2a and B3b, the Ephb4a receptor and the Pak2a kinase are required for the development of pharyngeal pouches and the segmentation of the posterior facial skeleton.
Essential in vivo role for betaPix and Pak2a during embryonic development and a previously unrecognized pathway specifically involved in cerebrovascular stabilization. [BetaPix AND Pak2a]
Data provide evidence for a critical function of Pak2 in vascular integrity and demonstrate a severe disease phenotype resulting from loss of Pak2 function.
Basement membrane proteins promote PAK2 Ser-20 phosphorylation through enhanced eNOS activation and NO production.
The p21 activated kinases (PAK) are critical effectors that link Rho GTPases to cytoskeleton reorganization and nuclear signaling. The PAK proteins are a family of serine/threonine kinases that serve as targets for the small GTP binding proteins, CDC42 and RAC1, and have been implicated in a wide range of biological activities. The protein encoded by this gene is activated by proteolytic cleavage during caspase-mediated apoptosis, and may play a role in regulating the apoptotic events in the dying cell.
, S6/H4 kinase
, p21 (CDKN1A)-activated kinase 2
, p21-activated kinase 2
, serine/threonine-protein kinase PAK 2
, p21 activated kinase 2
, p21-activated kinase I
, p21-activated protein kinase I