Protein Kinase Cdelta isozyme human, >95% (SDS-PAGE), recombinant, expressed in baculovirus infected insect cells, buffered aqueous glycerol solution

Synonyms: Ca2+-activated phospholipid-dependent serine-threonine kinase delta isozyme human; PKCdelta human

MDL No.: MFCD03458221

Purity: >95% (SDS-PAGE)

Storage: -70C

Enzyme Commission (EC) Number: 2.7.1.37  ( BRENDA | IUBMB )

UNSPSC Code: 12352200

Biochem/physiol Actions: 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 PKCalpha, betaI, betaII, and gamma. Members of the second family are phospholipid-dependent but Ca2+-independent, and include PKCdelta, epsilon, eta, and theta. Members of the third family are not activated by either DAG or phorbol esters and include PKCξ, mu, and iota.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.

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

Unit Definition: One unit will transfer 1 nmol of phosphate to PKC epsilon substrate peptide in 1 min at pH 7.4 at 30 C.