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Overview
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CLPS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 118 amino acids (18-112) and having a molecular mass of 12.5 kDa. CLPS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques. Colipase (CLPS) is a protein co-enzyme essential for optimal enzyme activity of pancreatic lipase. CLPS is secreted by the pancreas as an inactive form, procolipase, which is then activated in the intestinal lumen by trypsin. CLPS prevents the inhibitory effect of bile salts on the lipase-catalyzed intraduodenal hydrolysis of dietary long-chain triglycerides. CLPS allows lipase to anchor noncovalently to the surface of lipid micelles, counteracting the destabilizing influence of intestinal bile salts. CLPS binds to the C-terminal, non-catalytic domain of lipase, thus stabilizing an active conformation and significantly increasing the whole hydrophobic binding site.
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Overview