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Western blot analysis of PKCε on rat brain lysate. Lane 1: 1:1000, lane 2: 1:2000, lane 3: 1:4000 dilution of PKCε.
PKC epsilon (clone 21) staining on rat brain. Formalin fixed paraffin section with citrate buffer pretreatment. 40X
BD Transduction Laboratories™ Purified Mouse Anti-PKCε
BD Transduction Laboratories™ Purified Mouse Anti-PKCε
Regulatory Status Legend
Any use of products other than the permitted use without the express written authorization of Becton, Dickinson and Company is strictly prohibited.
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.
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 PKC activators Ca2], phospholipid, diacylglycerol, or phorbol ester. However, the novel PKC (nPKC) subfamily members (δ,η, η, and θ isoforms) and the atypical PKC (aPKC) subfamily members (ζ , ι , and λ isoforms) are Ca[2+] independent and lack the C2 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. Expression of the 90 kDa PKCα is induced by interferon-α. Generally, PKCα is expressed at very low levels in normal murine tissues, except brain. Overexpression of PKCα leads to increased growth rates and higher cell densities in monolayer cultures. A high level of expression is seen in several hematopoietic cell lines and tumors. This suggests a possible role for PKCα in tumorigenesis.
Development References (5)
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Balafanova Z, Bolli R, Zhang J. Nitric oxide (NO) induces nitration of protein kinase Cepsilon (PKCepsilon ), facilitating PKCepsilon translocation via enhanced PKCepsilon -RACK2 interactions: a novel mechanism of no-triggered activation of PKCepsilon. J Biol Chem. 2002; 277(17):15021-15027. (Clone-specific: ELISA, Immunoprecipitation, Western blot). View Reference
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Mischak H, Kolch W, Goodnight J. Expression of protein kinase C genes in hemopoietic cells is cell-type- and B cell-differentiation stage specific. 1999; 147(11):3981-3987. (Biology). View Reference
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Ohno S, Akita Y, Hata A. Structural and functional diversities of a family of signal transducing protein kinases, protein kinase C family; two distinct classes of PKC, conventional cPKC and novel nPKC. Adv Enzyme Regul. 1991; 31:287-303. (Biology). View Reference
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Ping P, Song C, Zhang J. Formation of protein kinase C(epsilon)-Lck signali. J Clin Invest. 2002; 109(4):499-507. (Clone-specific: Immunoprecipitation, Western blot). View Reference
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Zhu DM, Fang WH, Narla RK, Uckun FM. A requirement for protein kinase C inhibition for calcium-triggered apoptosis in acute lymphoblastic leukemia cells. Clin Cancer Res. 1999; 5(2):355-360. (Clone-specific: Immunofluorescence). View Reference
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