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.
PKCL, Recombinant (Human)
Kinase activity is measured as the molar amount of phosphate incorporated into the CREBtide substrate peptide per minute per mg protein at 30°C using a final concentration of 50 μM [32P] ATP.
recombinant, expressed in E. coli, > 85% (SDS-PAGE), buffered aqueous glycerol solution
buffered aqueous glycerol solution
apparent mol wt ~98 kDa
Solution of 5 μg in 50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 0.25 mM DTT, 0.1 mM EGTA, 0.1mM EDTA, 0.1 mM PMSF, and 25% glycerol.
Cell junction organization, organism-specific biosystem; Cell-Cell communication, organism-specific biosystem; Cell-cell junction organization, organism-specific biosystem; EGFR1 Signaling Pathway, organism-specific biosystem; Endocytosis, organism-specific biosystem; Endocytosis, conserved biosystem; G Protein Signaling Pathways, organism-specific biosystem
ATP binding; metal ion binding; nucleotide binding; phospholipid binding; protein binding; protein kinase C activity; protein kinase activity; protein serine/threonine kinase activity; protein serine/threonine kinase activity; zinc ion binding
PKCL; Protein Kinase C Lambda/Iota; PKCι