Recombinant human Protein Kinase C (PKC) zeta, 10 µg

Background: Protein kinase C (PKC) is a family of serine-threonine kinases, which are classified into three major groups: classical (α, β and γ), novel (δ, ε, η, and θ) and atypical (μ, ξ and ι).In contrast to classical isoforms PKC zeta (ξ ) exhibits a kinase activity which is independent of calcium and diacylglycerol but not of phosphatidylserine. Furthermore, it is insensitive to typical PKC inhibitors. Unlike the classical PKC isoenzymes, it has only a single zinc finger module. The ceramide binding domain (C20zeta) in the carboxyl terminus of PKC zeta has emerged as important binding partner for ceramide affecting the formation of junctional complexes in epithelial cells. Furthermore, pre-activation of PKC ξ by ceramide or ceramide analogs sensitizes the enzyme to inhibition by PAR-4, resulting in a down-regulation of NF-kB-dependent cell survival. 

Recombinant human Protein kinase C (PKC) zeta, recombinant and active enzyme, full lenght protein (amino acids G6-V584), N-terminally fused to GST-HIS6-Thrombin cleavage site

Theoretical MW: 99.65 kDa (fusion proteins)
Expression system: Baculovirus infected Sf9 cells
Purification: One-step affinity purification usingGSH-agarose
Storage buffer: 50 mM Tris-HCl, pH 8.0; 100 mM NaCl, 5 mM DTT, 15 mM reduced glutathione,
20% glycerol
Protein concentration: 0.181 mg/ml (Bradford method using BSA as standard protein)
Method for determination of Km value & specific activity: Filter binding assay MSFC membrane
Specific activity : 83,000 pmol/mg min

Entrez Gene ID: 5590
UniProtKB: Q05513

Ordering information: shipped on dry ice

Entrez Gene ID: 5590 
UniProtKB: Q05513

Product specific literature:

Hirai T, Chida K.(2003) „Protein kinase Czeta (PKCzeta): activation mechanisms and cellular functions.” J Biochem.;133(1):1-7.

Puls A, Schmidt S, Grawe F, Stabel S. (1997) “Interaction of protein kinase C zeta with ZIP, a novel protein kinase C-binding protein.” Proc Natl Acad Sci U S A. 10;94(12):6191-6.

Wang G, Krishnamurthy K, Umapathy NS, Verin AD, Bieberich E.(2009) „The carboxyl-terminal domain of atypical protein kinase Czeta binds to ceramide and regulates junction formation in epithelial cells.” J Biol Chem. 22;284(21):14469-75.

Wang G, Silva J, Krishnamurthy K, Tran E, Condie BG, Bieberich E.(2005) „Direct binding to ceramide activates protein kinase Czeta before the formation of a pro-apoptotic complex with PAR-4 in differentiating stem cells.” J Biol Chem. 15;280(28):26415-24.