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.
Does not require Ca2+ or phosphatidylserine for its activity.
> 800 units/mg protein
25 μg/mL protein
One unit will transfer of 1 nanomole of phosphate per minute at 30°C using Histone III as substrate and phosphatidylserine as an activator.
Storage buffer: 20 mM Tris-HCl, pH 7.5, 2 mM EGTA, 2 mM EDTA, 1 mM DTT, 10 mM potassium phosphate, 50% glycerol, 0.05% Triton™ X-100
Prepared by tryptic digestion of PKC.
B Cell Receptor Signaling Pathway, organism-specific biosystem; Calcium Regulation in the Cardiac Cell, organism-specific biosystem; EGFR1 Signaling Pathway, organism-specific biosystem; G Protein Signaling Pathways, organism-specific biosystem; Metabolism, organism-specific biosystem; Metabolism of lipids and lipoproteins, organism-specific biosystem; Myometrial Relaxation and Contraction Pathways, organism-specific biosystem
ATP binding; metal ion binding; nucleotide binding; protein kinase C activity; protein serine/threonine kinase activity; protein serine/threonine kinase activity
PKC-M, PKM; PKCM; Protein Kinase C Catalytic Subunit