Immunohistochemistry of paraffin-embedded human colon cancer using CSB-PA620966LA01HU at dilution of 1:100
Immunofluorescent analysis of HepG2 cells using CSB-PA620966LA01HU at dilution of 1:100 and Alexa Fluor 488-congugated AffiniPure Goat Anti-Rabbit IgG(H+L)
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貨期:
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用途:
For Research Use Only. Not for use in diagnostic or therapeutic procedures.
PKC-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. Plays a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion, tumor cell invasion and transcription activation signaling processes. Phosphorylates CTTN in hyaluronan-induced astrocytes and hence decreases CTTN ability to associate with filamentous actin. Phosphorylates HDAC5, therefore lead to impair HDAC5 import. Direct RhoA target required for the regulation of the maturation of primordial junctions into apical junction formation in bronchial epithelial cells. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Stimulates FYN kinase activity that is required for establishment of skin cell-cell adhesion during keratinocytes differentiation. Regulates epithelial bladder cells speed and direction of movement during cell migration and tumor cell invasion. Inhibits Akt pro-survival-induced kinase activity. Mediates Rho protein-induced transcriptional activation via the c-fos serum response factor (SRF). Involved in the negative regulation of ciliogenesis.; (Microbial infection) Phosphorylates HCV NS5B leading to stimulation of HCV RNA replication.
基因功能參考文獻(xiàn):
The expression of PKN2 in colon cancer cells suppresses tumor associated M2 macrophage polarization and tumor growth. PMID: 29368606
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. PMID: 28720584
Helicobacter pylori CagA interacts with PRK2 and inhibits its kinase activity. PMID: 26041307
findings demonstrate that Yersinia enterocolitica rYopM interacts with RSK1 and PRK2 following cell-penetration PMID: 25513777
Regulation of protein kinase C-related protein kinase 2 (PRK2) by an intermolecular PRK2-PRK2 interaction mediated by Its N-terminal domain. PMID: 22511787
these findings suggest that Hsp90 plays a critical role in the regulation of HCV RNA polymerase phosphorylation via the PDK1-PRK2 signaling pathway. PMID: 22490666
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. PMID: 20974804
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. PMID: 17332740
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. PMID: 17632197
Little evidence of association was observed between SNPs in PKN2 and type 2 diabetes in African Americans. PMID: 18443202
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 PMID: 18835241