Mouse Anti-PRKCH Recombinant Antibody (CBYC-P625) (CBMAB-P2850-YC)

Protein Kinase C Eta

Protein kinase C (PKC) is a family of serine-and threonine-specific protein kinases that can be activated by calcium and the second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. The protein encoded by this gene is one of the PKC family members. It is a calcium-independent and phospholipids-dependent protein kinase.

PKC-L; PKCL; PRKCL; nPKC-eta

Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in the regulation of cell differentiation in keratinocytes and pre-B cell receptor, mediates regulation of epithelial tight junction integrity and foam cell formation, and is required for glioblastoma proliferation and apoptosis prevention in MCF-7 cells. In keratinocytes, binds and activates the tyrosine kinase FYN, which in turn blocks epidermal growth factor receptor (EGFR) signaling and leads to keratinocyte growth arrest and differentiation. Associates with the cyclin CCNE1-CDK2-CDKN1B complex and inhibits CDK2 kinase activity, leading to RB1 dephosphorylation and thereby G1 arrest in keratinocytes. In association with RALA activates actin depolymerization, which is necessary for keratinocyte differentiation. In the pre-B cell receptor signaling, functions downstream of BLNK by up-regulating IRF4, which in turn activates L chain gene rearrangement. Regulates epithelial tight junctions (TJs) by phosphorylating occludin (OCLN) on threonine residues, which is necessary for the assembly and maintenance of TJs. In association with PLD2 and via TLR4 signaling, is involved in lipopolysaccharide (LPS)-induced RGS2 down-regulation and foam cell formation. Upon PMA stimulation, mediates glioblastoma cell proliferation by activating the mTOR pathway, the PI3K/AKT pathway and the ERK1-dependent phosphorylation of ELK1. Involved in the protection of glioblastoma cells from irradiation-induced apoptosis by preventing caspase-9 activation. In camptothecin-treated MCF-7 cells, regulates NF-kappa-B upstream signaling by activating IKBKB, and confers protection against DNA damage-induced apoptosis. Promotes oncogenic functions of ATF2 in the nucleus while blocking its apoptotic function at mitochondria. Phosphorylates ATF2 which promotes its nuclear retention and transcriptional activity and negatively regulates its mitochondrial localization.

Cell differentiationIEA:UniProtKB-KW
Intracellular signal transductionManual Assertion Based On ExperimentIBA:GO_Central
Negative regulation of glial cell apoptotic processManual Assertion Based On ExperimentIMP:UniProtKB
Peptidyl-serine phosphorylationManual Assertion Based On ExperimentIBA:GO_Central
Positive regulation of B cell receptor signaling pathwayManual Assertion Based On ExperimentIMP:UniProtKB
Positive regulation of glial cell proliferationManual Assertion Based On ExperimentIMP:UniProtKB
Positive regulation of keratinocyte differentiationISS:UniProtKB
Positive regulation of macrophage derived foam cell differentiationISS:UniProtKB
Positive regulation of NF-kappaB transcription factor activityManual Assertion Based On ExperimentIMP:UniProtKB
Positive regulation of protein localization to plasma membraneManual Assertion Based On ExperimentTAS:ParkinsonsUK-UCL
Protein kinase C signalingIEA:Ensembl
Protein phosphorylationManual Assertion Based On ExperimentIDA:UniProtKB
Regulation of bicellular tight junction assemblyManual Assertion Based On ExperimentIMP:UniProtKB
Signal transductionManual Assertion Based On ExperimentTAS:ProtInc

Cytoplasm

Ischemic stroke (ISCHSTR):
A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.