Host: Insect cells • AA: 18-112 • MW: 11.5 kDa
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Colipase (human, recombinant)

Item No. 37022

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
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 637 mM sodium chloride, 2.7 mM potassium chloride, 10 mM disodium phosphate, 1.8 mM monopotassium phosphate, 10% glycerol, pH 7.0, with 5% trehalose, 5% mannitol, and 0.01% Tween 80
Host
Insect cells
UniProt Accession №
P04118
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    100 µg

    $328

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    Product Description

    Colipase is a protein coenzyme required for the activity of pancreatic lipase.1,2 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.3,4 Colipase deficiency induces steatorrhea, the excretion of excess fat in stool.5 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.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Lowe, M.E. Structure and function of pancreatic lipase and colipase. Annu. Rev. Nutr. 17, 141-158 (1997).

    2. Borgström, B., Wieloch, T., and Erlanson-Albertsson, C. Evidence for a pancreatic pro-colipase and its activation by trypsin. FEBS Lett. 108(2), 407-410 (1979).

    3. van Tilbeurgh, H., Bezzine, S., Cambillau, C., et al. Colipase: Structure and interaction with pancreatic lipase. Biochim. Biophys. Acta 1441(2-3), 173-184 (1999).

    4. Ahmed, S.A., Ali, N., Qureshi, U., et al. Molecular dynamics simulation of human pancreatic lipase and lipase-colipase complex: Insight into the structural fluctuations and conformational changes. Int. J. Comput. Theor. Chem. 8(1), 19-26 (2020).

    5. Hildebrand, H., Borgström, B., Békássy, A., et al. Isolated co-lipase deficiency in two brothers. Gut 23(3), 243-246 (1982).