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| name: | Protein Kinase Cepsilon isozyme human |
| cat_no: | P1164 |
| gene id: | human PRKCE(5581) |
| brand: | SIGMA |
| prod_type: | Chemical |
| name_suffix: | >95% (SDS-PAGE), recombinant, expressed in baculovirus infected insect cells, buffered aqueous glycerol solution |
| storage temp.: | -70C |
| storage: | -70C |
| form: | buffered aqueous glycerol solution |
| physical form: | 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 |
| shipped in: | dry ice |
| syns: | Ca2+-activated phospholipid-dependent serine-threonine kinase, epsilon isozyme human; PKCepsilon human |
| unspsc_code: | 12352204 |
| wgk: | 1 |
| mdl_no: | MFCD03458222 |
| mol wt: | apparent mol wt 89-96 kDa |
| 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. |
| purity: | >95% (SDS-PAGE) |
| assay: | >95% (SDS-PAGE) |
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more information: | company product webpage |
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