CST, 9375T, Phospho-PKC alpha/beta II (Thr638/641) Antibody

Polyclonal Antibody for studying PKCalpha (Thr638) phosphate/PKCbeta2 (Thr641) phosphate. Validated for Western Blotting. Available in 2 sizes. Highly specific and rigorously validated in-house, Phospho-PKC alpha/beta II (Thr638/641) Antibody (CST #9375) is ready to ship. Product Usage Information Western Blotting: 1:1000 Storage Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at -20°C. Do not aliquot the antibody. Protocol Available protocols: Western Blotting Specificity / Sensitivity Phospho-PKC alpha/beta II (Thr638/641) Antibody detects PKC alpha only when phosphorylated at threonine 638 and PKC beta II only when phosphorylated at threonine 641. This antibody also reacts with gamma. Species Reactivity: Human, Mouse, Monkey Source / Purification Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr638 of human PKC alpha. Antibodies are purified by protein A and peptide affinity chromatography. 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). Alternate Names AAG6; aging-associated gene 6; KPCA; KPCB; MGC129900; MGC129901; MGC41878; PKC beta 2; PKC beta II; PKC beta2; PKC-A; PKC-alpha; PKC-B; PKC-beta; PKC-beta II; PKCA; PKCalpha; PKCB; PKCB iso2; PKCbeta; PKCI(2); PKCI+/-; PRKACA; PRKCA; PRKCB; PRKCB1; PRKCB2; protein kinase C; protein kinase C alpha; Protein kinase C alpha type; protein kinase C beta; protein kinase C beta 1; Protein kinase C beta type; protein kinase C, alpha; protein kinase C, beta; protein kinase C, beta 1 polypeptide Specification REACTIVITY: H M Mk SENSITIVITY: Endogenous MW (kDa): 80, 82 SOURCE: Rabbit