|Application ||WB, IHC, IF|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||76869 Da|
|Other Names||Protein kinase C beta type, PKC-B, PKC-beta, PRKCB, PKCB, PRKCB1|
|Target/Specificity||A synthetic peptide corresponding to residues near C-terminus of human PKC beta-II was used as immunogen. The antibody does not cross-react with human PKC beta-I. Predicted to cross-react with bovine PKC beta, and pig PKC beta-II, based on sequence homology|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||PKC beta II Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||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. May participate in the regulation of glucose transport in adipocytes by negatively modulating the insulin-stimulated translocation of the glucose transporter SLC2A4/GLUT4. 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 (By similarity). Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription.|
|Cellular Location||Cytoplasm. Nucleus. Membrane; Peripheral membrane protein|
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Provided below are standard protocols that you may find useful for product applications.
PKCβII is a member of the serine/threonine protein kinase C (PKC) family (1) that includes 10 closely related isozymes classified as the conventional, the novel and the atypical. The conventional PKCβII is implicated in diverse cellular process including secretion, proliferation, differentiation, apoptosis, permeability, migration & hypertrophy (2-3). PKCβII structure consists of a C-terminal catalytic region, containing an activator-binding domain and a Ca2+-binding domain, and a regulatory domain. The catalytic domain is activated by undergoing multiple serine/threonine and tyrosine phosphorylation that are either autocatalytic, or catalyzed by PKC kinases (4). PKCβII and PKCβI differ only in their C-terminal (5).
1. Coussens L, Parker PJ, Rhee L, Yang-Feng TL, Chen E, Waterfield MD, Francke U, Ullrich A. (986) Science. Aug 22;233(4766):859-66.
2. Mellor, H., and Parker, P. J. (1998) Biochem. J. 332, 281-292
3. Nishizuka, Y. (1995) FASEB J. 9, 484-496
4. Parekh, D. B., Ziegler, W., and Parker, P. J. (2000) EMBO J. 19, 496-503
5. YS Niino, S Ohno and K Suzuki. (1992) J. Biol. Chem., Vol. 267, Issue 9, 6158-6163, 03
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