K117453P Anti-PRKCB Polyclonal

Calcium-activated， phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase involved in various cellular processes such as regulation of the B-cell receptor (BCR) signalosome， oxidative stress-induced apoptosis， androgen receptor-dependent transcription regulation， insulin signaling and endothelial cells proliferation. Plays a key role in B-cell activation by regulating BCR-induced NF-kappa-B activation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11/CARMA1 at ’Ser-559’， ’Ser-644’ and ’Ser-652’. Phosphorylation induces CARD11/CARMA1 association with lipid rafts and recruitment of the BCL10-MALT1 complex as well as MAP3K7/TAK1， which then activates IKK complex， resulting in nuclear translocation and activation of NFKB1. Plays a direct role in the negative feedback regulation of the BCR signaling， by down-modulating BTK function via direct phosphorylation of BTK at ’Ser-180’， which results in the alteration of BTK plasma membrane localization and in turn inhibition of BTK activity. Involved in apoptosis following oxidative damage: in case of oxidative conditions， specifically phosphorylates ’Ser-36’ of isoform p66Shc of SHC1， leading to mitochondrial accumulation of p66Shc， where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (ANDR)-dependent transcription， by being recruited to ANDR target genes and specifically mediating phosphorylation of ’Thr-6’ of histone H3 (H3T6ph)， a specific tag for epigenetic transcriptional activation that prevents demethylation of histone H3 ’Lys-4’ (H3K4me) by LSD1/KDM1A. In insulin signaling， may function downstream of IRS1 in muscle cells and mediate insulin-dependent DNA synthesis through the RAF1-MAPK/ERK signaling cascade. Participates in the regulation of glucose transport in adipocytes by negatively modulating the insulin-stimulated translocation of the glucose transporter SLC2A4/GLUT4. Phosphorylates SLC2A1/GLUT1， promoting glucose uptake by SLC2A1/GLUT1. Under high glucose in pancreatic beta-cells， is probably involved in the inhibition of the insulin gene transcription， via regulation of MYC expression. In endothelial cells， activation of PRKCB induces increased phosphorylation of RB1， increased VEGFA-induced cell proliferation， and inhibits PI3K/AKT-dependent nitric oxide synthase (NOS3/eNOS) regulation by insulin， which causes endothelial dysfunction. Also involved in triglyceride homeostasis. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN， activating transcription.