Protein Kinase Cζ isozyme human

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.

PKC ε can transfer 1100 nmole of phosphate to PKC ε substrate peptide per minute per mg of total protein at 30 °C.

One unit will transfer 1 nanomole of phosphate to PKC epsilon substrate peptide per minute at pH 7.5 at 30 deg C.

Solution in 20 mM HEPES, pH 7.5; 2 mM EDTA, 2 mM EGTA, 5 mM DTT, 250 mM NaCl, 0.05% Triton X-100, and 50% glycerol.