Recombinant human Protein kinase C (PKC) gamma, 10 µg

Background: Protein kinase C (PKC) is a family of serine-threonine kinases, which are classified into three major groups: classical PKC (α, β and γ), novel PKC (δ, ε, η, and θ) and atypical PKC (μ, ξ and ι).PKCγ consists of a C-terminal kinase domain and a N-terminal regulatory domain, formed by C1 domains (C1A and C1B) and a C2 domain. Activation of PKC gamma involves recruitment to the membrane and interaction with phospholipids, Ca2+ and diacylglycerol. Furthermore, fully active protein results upon phosphorylation of the activation loop. PKCγ shows a unique neuronal distribution and intracellular localization in brain cells, neuronal tissues, retina, and lens and is important for stress response in neurological tissues and modulates neurotransmission and cell survival.

Recombinant human PKC-gamma, Amino acids M1-M697 (full lenght), N-terminally fused to GSTHIS6-Thrombin cleavage site

Expression: Baculovirus infected Sf9 cells
Storage buffer: 50 mM Tris-HCl, pH 8.0; 100 mM NaCl, 5 mM DTT, 15 mM reduced glutathione, 20% glycerol
Protein concentration: 0.088 μg/μl(Bradford method using BSA as standard protein)
Method for determination of Km value & Specific activity: Filter binding assay MSPH membrane
Specific activity: 325, 000 pmol/mg x min

Entrez Gene ID: 5582 
UniProtKB: P05129

Ordering information: shipped on dry ice

Product specific literature:

Tuttle KR. (2008) "Protein kinase C-beta inhibition for diabetic kidney disease." Diabetes Res Clin Pract. 13;82

Avignon A, Sultan A. (2006) "PKC-B inhibition: a new therapeutic approach for diabetic complications?" Diabetes Metab. 32(3):205-13.

Carroll MP, May WS (1994) "Protein kinase C-mediated serine phosphorylation directly activates Raf-1 in murine hematopoietic cells" J Biol Chem 269(2):1249-56

Newton AC (1995) "Protein kinase C: structure, function, and regulation" J Biol Chem. 270(48):28495-8

Newton AC (1997) "Regulation of protein kinase C" Curr Opin Cell Biol. 9(2):161-7

Kawakami T, Kawakami Y, Kitaura J. (2002) " Protein kinase C beta (PKC beta): normal functions and diseases." J Biochem.;132 (5):677-82.

Idris I, Donnelly R. (2006) " Protein kinase C beta inhibition: A novel therapeutic strategy for diabetic microangiopathy." Diab Vasc Dis Res.;3(3):172-8

Corbalan-Garcia S, Gomez-Fernandez JC. (2006) "Protein kinase C regulatory domains: the art of decoding many different signals in membranes." Biochim Biophys Acta. 1761(7):633-54.