Protein Kinase C, theta (PRKCQ) (AA 21-217) antibody

Antigen: Protein Kinase C, theta (PRKCQ)

Synonyms: PRKCT, MGC126514, MGC141919, nPKC-theta

Binding Site: AA 21-217

Clonality: Monoclonal (27)

Host: Mouse

Reactivity: Human

Conjugate: Un-conjugated

Application: Western Blotting (WB), Immunofluorescence (IF), Immunoprecipitation (IP)

Catalog no.: ABIN967738

Additional Information

Alternative name: PKC theta

Immunogen: Human PKCtheta

Format: Liquid

Isotype: IgG2a, kappa

Clone: 27

Description: The Protein Kinase C (PKC) family of homologous serine/threonine protein kinases is involved in a number of processes, such as growth, differentiation, and cytokine secretion. At least eleven isozymes have been described. These proteins are products of multiple genes and alternative splicing. PKC consists of a single polypeptide chain containing four conserved regions (C) and five variable regions (V). The N-terminal half containing C1, C2, V1, and V2 constitutes the regulatory domain and interacts with the PKC activators Ca2+, phospholipid, diacylglycerol, or phorbol ester. However, the novel PKC (nPKC) subfamily members (delta, epsilon, eta, and theta isoforms) and the atypical PKC (aPKC) subfamily members (zeta, iota, and lambda isoforms) are Ca2+-independent and lack the C2 domain. The aPKC members are unique in that their activity is independent of diacylglycerols and phorbol esters. They also lack one repeat of the cysteine-rich sequences that are conserved in cPKC and nPKC members. The C-terminal region of PKC contains the catalytic domain. The PKC pathway represents a major signal transduction system that is activated following ligand-stimulation of transmembrane receptors by hormones, neurotransmitters, and growth factors. PKCtheta transcripts are expressed in most tissues with the highest levels being found in hematopoietic tissues and cell lines, including T cells and thymocytes. PKCtheta mRNA is readily detectable in skeletal muscle, lung and brain. However, PKCtheta expression is not detected in several human carcinoma cell lines. Abundant expression of this PKC isozyme in hematopoietic cells suggest that it may have a role in growth and differentiation processes of these cells. This antibody is routinely tested by western blot analysis.

Characteristics: 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.

Molecular Weight: 79 kDa

Comments:

Related Products: ABIN968537, ABIN967389

Application Details

Concentration: 250 µg/ml

Purity: Purified

Purification: Purified from tissue culture supernatant or ascites by affinity chromatography.

Buffer: Aqueous buffered solution containing BSA, glycerol.

Preservative: 0.09% Sodium azide.

Storage: Store undiluted at -20° C.

Research Area: Cancer

Restrictions: For Research Use only

Images

Western blot analysis of PKCtheta on a Jurkat lysate. Lane 1: 1:250, lane 2: 1:500, lane 3: 1:1000 dilution of the anti- human PKCtheta antibody.

Immunofluorescence staining of A431 cells.

Publications

Product: Soderling: "Protein kinases. Regulation by autoinhibitory domains." in: The Journal of biological chemistry, Vol. 265, Issue 4, pp. 1823-6, 1990 (PubMed).

Nishizuka: "The molecular heterogeneity of protein kinase C and its implications for cellular regulation." in: Nature, Vol. 334, Issue 6184, pp. 661-5, 1988 (PubMed).

Villalba, Coudronniere, Deckert et al.: "A novel functional interaction between Vav and PKCtheta is required for TCR-induced T cell activation." in: Immunity, Vol. 12, Issue 2, pp. 151-60, 2000 (PubMed).

Dienz, Hehner, Droge et al.: "Synergistic activation of NF-kappa B by functional cooperation between vav and PKCtheta in T lymphocytes." in: The Journal of biological chemistry, Vol. 275, Issue 32, pp. 24547-51, 2000 (PubMed).

Villalba, Bi, Rodriguez et al.: "Vav1/Rac-dependent actin cytoskeleton reorganization is required for lipid raft clustering in T cells." in: The Journal of cell biology, Vol. 155, Issue 3, pp. 331-8, 2001 (PubMed).