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.
Companion Products
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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. 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 ( δ, ε, η, and θ isoforms) and the atypical PKC (aPKC) subfamily members (ζ, ί, and λ 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. 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. PKCλ shows the highest degree of amino acid homology with PKCζ (72%) and PKCλ mRNA is expressed in a variety of cells and tissues. The PKCλ protein kinase is capable of autophosphorylation and can be activated by phosphatidylserine, but not by other PKC activators such as diacylglycerols, Ca2+, or phorbol esters.
Development References (5)
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Akimoto K, Mizuno K, Osada S. A new member of the third class in the protein kinase C family, PKC lambda, expressed dominantly in an undifferentiated mouse embryonal carcinoma cell line and also in many tissues and cells. J Biol Chem. 1994; 269(17):12677-12683. (Biology). View Reference
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Jain N, Zhang T, Kee WH, Li W, Cao X. Protein kinase C delta associates with and phosphorylates Stat3 in an interleukin-6-dependent manner. J Biol Chem. 1999; 274(34):24392-24400. (Clone-specific: Immunoprecipitation, Western blot). View Reference
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Pauken CM, Capco DG. The expression and stage-specific localization of protein kinase C isotypes during mouse preimplantation development. Dev Biol. 2000; 223(2):411-421. (Clone-specific: Immunofluorescence, Western blot). View Reference
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Trauzold A, Wermann H, Arlt A. CD95 and TRAIL receptor-mediated activation of protein kinase C and NF-kappaB contributes to apoptosis resistance in ductal pancreatic adenocarcinoma cells. Oncogene. 2001; 20(31):4258-4269. (Clone-specific: Western blot). View Reference
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Uberall F, Giselbrecht S, Hellbert K. Conventional PKC-alpha, novel PKC-epsilon and PKC-theta, but not atypical PKC-lambda are MARCKS kinases in intact NIH 3T3 fibroblasts. J Biol Chem. 1997; 272(7):4072-4078. (Clone-specific: In vitro kinase assay). View Reference
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For Research Use Only. Not for use in diagnostic or therapeutic procedures.