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anti-Human PKN2 Antibodies:
anti-Mouse (Murine) PKN2 Antibodies:
anti-Rat (Rattus) PKN2 Antibodies:
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Human Monoclonal PKN2 Primary Antibody for 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. in Annals of internal medicine 2009
The expression of PKN2 in colon cancer cells suppresses tumor associated M2 macrophage polarization and tumor growth.
Steady-state kinetic analysis revealed that PKN1-3 follows a sequential ordered Bi-Bi 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 glycogen, and oxidation. Thus, PKN2 alters key signaling pathways and transcriptional networks to regulate glucose and lipid metabolism.
Helicobacter pylori CagA interacts with PRK2 and inhibits its kinase activity.
TXA2-mediated neoplastic responses in prostate adenocarcinoma PC-3 cells occur through a PRK1/PRK2-dependent mechanism.
findings demonstrate that Yersinia enterocolitica rYopM interacts with RSK1 and PRK2 following cell-penetration
Regulation of protein kinase C-related protein kinase 2 (PRK2) by an intermolecular PRK2-PRK2 interaction mediated by Its N-terminal domain.
these findings suggest that Hsp90 plays a critical role in the regulation of HCV RNA polymerase phosphorylation via the PDK1-PRK2 signaling pathway.
PKN 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.
PRK2/PKN2, is an essential regulator of both entry into mitosis and exit from cytokinesis in HeLa S3 cells, required for abscission of the midbody at the end of the cell division cycle and for phosphorylation and activation of Cdc25B.
These observations highlight elements of Nef's functional complexity and demonstrate previously unsuspected structural requirements for PAK-2 activation and MHC-1 down-modulation in Nef's flexible N- and C-terminal regions.
Little evidence of association was observed between SNPs in PKN2 and type 2 diabetes in African Americans.
the last seven amino acid residues at the C-terminus of PRK2 are not required for the activation of the kinase by RhoA in vitro, however, the extreme C-terminal segment is critical for the full activation of PRK2 by RhoA in cells
In mature skeletal muscle, in vivo PKN2 knockdown decreased glucose uptake and increased AMPK 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 and PRK2 to negatively regulate pyrin by phosphorylation.
PKN2 formed complexes with Cdo, APPL1 and AKT via its C-terminal region and this interaction appeared to be important for induction of AKT 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 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