CST, 2998T, PKC iota/lambda (C83H11) Rabbit Monoclonal Antibody

Monoclonal Antibody for studying PKCiota. Validated for Western Blotting. Available in 2 sizes. Highly specific and rigorously validated in-house, PKC iota/lambda (C83H11) Rabbit Monoclonal Antibody (CST #2998) 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, 50% glycerol and less than 0.02% sodium azide. Store at -20°C. Do not aliquot the antibody. Protocol Available protocols: Western Blotting Specificity / Sensitivity PKC iota/lambda (C83H11) Rabbit Monoclonal Antibody detects endogenous levels of total PKCι/λ. This antibody does not cross-react with other PKC isoforms. Species Reactivity: Human, Mouse, Rat, Monkey Source / Purification Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Val200 of human PKCι/λ. 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). PKCι/λ (iota/lambda) is an atypical PKC that has recently been identified as an oncogene. The corresponding gene is amplified in many types of cancer and protein expression is essential for transformed cell growth, making this protein an attractive therapeutic target (8). Alternate Names aPKC-lambda/iota; Atypical protein kinase C-lambda/iota; DXS1179E; KPCI; MGC26534; nPKC-iota; PKC iota; PKCI; PRKC-lambda/iota; PRKCI; protein kinase C iota; Protein kinase C iota type; protein kinase C, iota Specification REACTIVITY: H M R Mk SENSITIVITY: Endogenous MW (kDa): 78 Source/Isotype: Rabbit IgG