Preparation And Storage
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- 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.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
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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. Conventional PKC (cPKC) subfamily members (α, β, and γ isoforms) 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 the C2-like domains of novel PKC (nPKC) subfamily members (δ, ε, η, and θ isoforms) are Ca2+-independent. The atypical PKC (aPKC) subfamily members (ζ, ι, and λ isoforms) lack the C2 domain and 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. PKCθ transcripts are expressed in most tissues with the highest levels being found in hematopoietic tissues and cell lines, including T cells and thymocytes. PKCθ mRNA is readily detectable in skeletal muscle, lung and brain. However, PKCθ 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.
The 27/PKCθ monoclonal antibody recognizes the C2-like domain of human PKCθ, regardless of phosphorylation status.
This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.
Development References (5)
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Dienz O, Hehner SP, Droge W, Schmitz ML. Synergistic activation of NF-kappa B by functional cooperation between vav and PKCtheta in T lymphocytes. J Biol Chem. 2000; 275(32):24547-24551. (Biology: Immunoprecipitation, Western blot). View Reference
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Nishizuka Y. The molecular heterogeneity of protein kinase C and its implications for cellular regulation. Nature. 1988; 334(6184):661-665. (Biology). View Reference
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Soderling TR. Protein kinases. Regulation by autoinhibitory domains. J Biol Chem. 1990; 265(4):1823-1826. (Biology). View Reference
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Villalba M, Bi K, Rodriguez F, Tanaka Y, Schoenberger S, Altman A. Vav1/Rac-dependent actin cytoskeleton reorganization is required for lipid raft clustering in T cells. J Cell Biol. 2001; 155(3):331-338. (Biology: Immunofluorescence). View Reference
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Villalba M, Coudronniere N, Deckert M, Teixeiro E, Mas P, Altman A. A novel functional interaction between Vav and PKCtheta is required for TCR-induced T cell activation. Immunity. 2000; 12(2):151-160. (Biology: Immunoprecipitation, In vitro kinase assay, Western blot). View Reference
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For Research Use Only. Not for use in diagnostic or therapeutic procedures.