Protein Kinase Cε isozyme human 

One unit will transfer 1 nmol of phosphate to PKC ε substrate peptide in 1 min at pH 7.4 at 30 °C.

Solution in 20mM HEPES, pH 7.4; 2mM EDTA, 2 mM EGTA, 5mM DTT, 100 mM NaCl, 0.05% Triton X-100, and 50% glycerol

Protein Kinase C (PKC) is a serine/threonine kinase that is activated intracellularly by signal transduction pathways that produce DAG from phosphatidylinositol diphosphate (PIP₂) and phosphatidylcholine (PC) through the action of various activated phospholipases. Phorbol esters also stimulate PKC. At least 11 PKC isozymes have been identified that differ in primary structure, tissue distribution, subcellular localization, response to extracellular signals, and substrate specificity. The isozymes can be grouped into three subfamilies. Members of the first family require Ca²⁺ and phospholipid and include PKCα, βI, βII, and γ. Members of the second family are phospholipid-dependent but Ca²⁺-independent, and include PKCδ, ε, η, and θ. Members of the third family are not activated by either DAG or phorbol esters and include PKCξ, μ, and ι.
Phosphorylation appears to be an important mechanism of regulation of all PKCs. PKC plays a role in the regulation of cell transformation, growth, differentiation, ruffling, vesicle trafficking, apoptosis and gene expression.

expressed in baculovirus infected insect cells

>95% (SDS-PAGE)

buffered aqueous glycerol solution

apparent mol wt 89-96 kDa

human ... PRKCE(5581)

dry ice

−70°C

Newton, A.C., Protein kinase C: structure, function, and regulation. J. Biol. Chem. 270, 28495, (1995)

Shiroshita, N., et al., Involvement of protein kinase C-epsilon in signal transduction of thrombopoietin in enhancement of interleukin-3-dependent proliferation of primitive hematopoietic progenitors. J. Pharmacol. Exp. Ther. 297, 868, (2001)

Vondriska, T.M., et al., Use of functional proteomics to investigate PKC epsilon-mediated cardioprotection: the signaling module hypothesis. Am. J. Physiol. Heart Circ. Physiol. 280, 1434-1441, (2001)

Shinohara, H., et al., A protective role of PKCepsilon against TNF-related apoptosis-inducing ligand (TRAIL)-induced apoptosis in glioma cells. Biochem. Biophys. Res. Commun. 284, 1162, (2001)

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