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anti-Human PKN2 Anticorps:
anti-Mouse (Murine) PKN2 Anticorps:
anti-Rat (Rattus) PKN2 Anticorps:
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Human Monoclonal PKN2 Primary Antibody pour FACS, IHC - ABIN969363
Cornelis, Qi, Zhang, Kraft, Manson, Cai, Hunter, Hu: Joint effects of common genetic variants on the risk for type 2 diabetes in U.S. men and women of European ancestry. dans Annals of internal medicine 2009
Steady-state kinetic analysis revealed that PKN1 (Montrer PKN1 Anticorps)-3 follows a sequential ordered Bi-Bi (Montrer CACNA1A Anticorps) kinetic mechanism, where peptide substrate binding is preceded by ATP binding. This kinetic mechanism was confirmed by additional kinetic studies for product inhibition and affinity of small molecule inhibitors.
PKN2 knockdown in vitro decreased insulin-stimulated glucose uptake, incorporation into glyco (Montrer PRKAA1 Anticorps)gen, and oxidation. Thus, PKN2 alters key signaling pathways and transcriptional networks to regulate glucose and lipid metabolism.
Helicobacter pylori CagA (Montrer S100A8 Anticorps) interacts with PRK2 and inhibits its kinase activity.
TXA2 (Montrer TBXA2R Anticorps)-mediated neoplastic responses in prostate adenocarcinoma PC-3 (Montrer PCSK1 Anticorps) cells occur through a PRK1 (Montrer PKN1 Anticorps)/PRK2-dependent mechanism.
findings demonstrate that Yersinia enterocolitica rYopM interacts with RSK1 (Montrer RPS6KA1 Anticorps) and PRK2 following cell-penetration
Regulation of protein kinase C-related (Montrer PKN1 Anticorps) protein kinase 2 (Montrer PKC Anticorps) (PRK2) by an intermolecular PRK2-PRK2 interaction mediated by Its N-terminal domain.
these findings suggest that Hsp90 (Montrer HSP90 Anticorps) plays a critical role in the regulation of HCV RNA polymerase phosphorylation via the PDK1 (Montrer PDK1 Anticorps)-PRK2 signaling pathway.
PKN (Montrer PKN1 Anticorps) isoforms are not simply redundant in supporting migration, but appear to be linked through isoform specific regulatory domain properties to selective upstream signals. It
Rho binding is essential for PRK2 function and facilitates PRK2 recruitment to junctions. Kinase-dead PRK2 acts as a dominant-negative mutant and prevents apical junction formation.
Protein kinase C-related kinase targets nuclear localization signals in a subset of class IIa histone deacetylases.
In mature skeletal muscle, in vivo PKN2 knockdown decreased glucose uptake and increased AMPK (Montrer PRKAA1 Anticorps) phosphorylation. Thus, PKN2 alters key signaling pathways and transcriptional networks to regulate glucose and lipid metabolism.
Mechanistically, Yersinia pseudotuberculosis YopM recruits and activates the mouse host kinases PRK1 (Montrer PKN1 Anticorps) and PRK2 to negatively regulate pyrin (Montrer MEFV Anticorps) by phosphorylation.
PKN2 formed complexes with Cdo (Montrer CDO1 Anticorps), APPL1 (Montrer APPL1 Anticorps) and AKT (Montrer AKT1 Anticorps) via its C-terminal region and this interaction appeared to be important for induction of AKT (Montrer AKT1 Anticorps) activity as well as myoblast differentiation.
To unravel the in vivo physiological function of PKN2, we targeted the PKN2 gene. Constitutive disruption of the mouse PKN2 gene resulted in growth retardation and lethality before embryonic day (E) 10.5. PKN2(-/-) embryo did not undergo axial turning and showed insufficient closure of the neural tube.Mouse embryonic fibroblasts (MEFs) derived from PKN2(-/-) embryos at E9.5 failed to grow.
Yersinia pseudotuberculosis mutants expressing YopM proteins unable to interact with either RSK1 (Montrer RPS6KA1 Anticorps) or PRK2 were defective for virulence in this assay, indicating that both interaction domains are important for YopM to promote pathogenesis.
phospholipid-regulated protein kinase, phosphorylates ribosomal protein S6\; may play a role in hepatic regulation
, cardiolipin-activated protein kinase Pak2
, protein kinase C-like 2
, protein-kinase C-related kinase 2
, serine/threonine-protein kinase N2
, serine/threonine kinase 7
, p140 kinase
, protease-activated kinase 2
, protein kinase N2
, protein kinase C-related kinase 2
, serine/threonine-protein kinase N2-like