Recombinant human Protein kinase C (PKC) beta 2, 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). PKCβ2 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 beta 2 involves recruitment to the membrane and interaction with phospholipids, Ca2+ and diacylglycerol. Furthermore, fully active protein results upon phosphorylation of the activation loop. PKCβ is expressed in pancreatic islet cells, monocytes, brain, and many vascular tissues, including retina, kidney and heart and dysregulation is associated with pathogenic processes involved in diabetic microangiopathy such as ischaemia, leakage, neovascularisation and abnormal vasodilator function. The two isoforms, PKC beta 1 and PKC beta 2, are generated by alternative splicing from a single gene and differ at their C-terminus.

Purified human recombinant protein kinase C beta 2 (PKCβ2) containing amino acids 1-673,  N-terminally fused to GST-Thrombin cleavage site

Theoretical MW (PKC-beta2): 103.7 kDa (fusion protein)
Expression system: Baculovirus infected Sf9 cells
Purification: One-step affinity purification using GSH-agarose
Storage buffer: 50 mM Tris-HCl, pH 8.0; 100 mM NaCl, 5 mM DTT, 15 mM reduced   glutathione, 20% glycerol
Protein concentration: 0.145 mg/ml (Bradford method using BSA as standard protein)
Method for determination of Km value & specific activity: Filter binding assay MAFC membrane
Specific activity: 320,000 pmol/mg x min

Entrez Gene ID: 5579   
UniProtKB: P05771

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

Corbalán-García S, Gómez-Fernández  JC. (2006) "Protein kinase C regulatory domains: the art of decoding many different signals in membranes." Biochim Biophys Acta. 1761(7):633-54.