CST, 25453S, PKC betaII (D9S2U) Rabbit Monoclonal Antibody

Monoclonal Antibody for studying PKCbeta2. Validated for Western Blotting,Immunoprecipitation,Flow Cytometry (Fixed/Permeabilized). Available in 2 sizes. Highly specific and rigorously validated in-house, PKC betaII (D9S2U) Rabbit Monoclonal Antibody (CST #25453) is ready to ship. Product Usage Information Western Blotting: 1:1000 Immunoprecipitation: 1:100 Flow Cytometry (Fixed/Permeabilized): 1:400 Storage Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at -20°C. Do not aliquot the antibody. Protocol Available protocols: Western Blotting, Immunoprecipitation, Flow Cytometry (Fixed/Permeabilized) Specificity / Sensitivity PKC betaII (D9S2U) Rabbit Monoclonal Antibody recognizes endogenous levels of total PKCβII protein. This antibody does not cross-react with PKCβI protein. Species Reactivity: Human, Mouse, Rat Source / Purification Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Val647 of human PKCβII protein. Background Activation of protein kinase C (PKC) is one of the earliest events in a cascade that controls a variety of cellular responses, including secretion, gene expression, proliferation, and muscle contraction (1,2). PKC isoforms belong to three groups based on calcium dependency and activators. Classical PKCs are calcium-dependent via their C2 domains and are activated by phosphatidylserine (PS), diacylglycerol (DAG), and phorbol esters (TPA, PMA) through their cysteine-rich C1 domains. Both novel and atypical PKCs are calcium-independent, but only novel PKCs are activated by PS, DAG, and phorbol esters (3-5). Members of these three PKC groups contain a pseudo-substrate or autoinhibitory domain that binds to substrate-binding sites in the catalytic domain to prevent activation in the absence of cofactors or activators. Control of PKC activity is regulated through three distinct phosphorylation events. Phosphorylation occurs at Thr500 in the activation loop, at Thr641 through autophosphorylation, and at the carboxy-terminal hydrophobic site Ser660 (2). Atypical PKC isoforms lack hydrophobic region phosphorylation, which correlates with the presence of glutamic acid rather than the serine or threonine residues found in more typical PKC isoforms. The enzyme PDK1 or a close relative is responsible for PKC activation. A recent addition to the PKC superfamily is PKCμ (PKD), which is regulated by DAG and TPA through its C1 domain. PKD is distinguished by the presence of a PH domain and by its unique substrate recognition and Golgi localization (6). PKC-related kinases (PRK) lack the C1 domain and do not respond to DAG or phorbol esters. Phosphatidylinositol lipids activate PRKs, and small Rho-family GTPases bind to the homology region 1 (HR1) to regulate PRK kinase activity (7). PKCβ has two isoforms, PKCβI and PKCβII, due to alternative splicing (8). Alternate Names KPCB; MGC41878; PKC beta 2; PKC beta II; PKC beta2; PKC-B; PKC-beta; PKC-beta II; PKCB; PKCB iso2; PKCbeta; PKCI(2); PRKCB; PRKCB1; PRKCB2; protein kinase C beta; protein kinase C beta 1; Protein kinase C beta type; protein kinase C, beta; protein kinase C, beta 1 polypeptide Specification REACTIVITY: H M R SENSITIVITY: Endogenous MW (kDa): 80 Source/Isotype: Rabbit IgG