Colipase (human, recombinant)

Colipase is a protein coenzyme required for the activity of pancreatic lipase. It is a polypeptide secreted by the pancreas as inactive pro-colipase, which is activated via removal of a 5-amino acid pro-peptide by trypsin in the intestines. Colipase binds to the C-terminus of pancreatic lipase to facilitate hydrolysis of dietary triglycerides in the presence of bile salts. Colipase deficiency induces steatorrhea, the excretion of excess fat in stool. Cayman's Colipase (human, recombinant) protein consists of 105 amino acids, has a calculated molecular weight of 11.5 kDa, and a predicted N-terminus of Ala18 after signal peptide cleavage.Purity: >90% estimated by SDS-PAGE. Endotoxin Testing: <1.0 EU/µg, determined by the LAL endotoxin assay. Source: Recombinant human C-terminal His-tagged colipase expressed in insect cells. Amino Acids: 18-112. MW: 11.5 kDa. Formulation: (Request formulation change), Lyophilized from sterile PBS, pH 7.0, 500 mM sodium chloride, and 10% glycerol. Host: Insect cells. UniProt Accession #: P04118.