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C3028

Sigma-Aldrich

Colipase from porcine pancreas

essentially salt-free, lyophilized powder

Synonym(s):

Colipase from hog pancreas

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About This Item

CAS Number:
55126-92-6
EC Number:
259-490-1
MDL number:
MFCD00130823
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

Porcine pancreas

Quality Level

200

Assay

≥95% (Lowry)

form

essentially salt-free, lyophilized powder

concentration

≥500 μ protein/vial

color

white to faint yellow

solubility

H2O: soluble 1.9-2.1 mg/mL, clear, colorless to faintly yellow

suitability

suitable for molecular biology

UniProt accession no.

P02703

application(s)

food and beverages

storage temp.

−20°C

Gene Information

pig ... CLPS(397407)

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General description

Research Area: Cell Signaling
Colipase is a member of a group of small cysteine-rich proteins characterized by a limited secondary structure. Its structure is relatively flat, measuring 25×30×35 Å, resembling an arrangement of protruding fingers interconnected at one end by a complex network of five disulfide bridges. The colipase structure comprises two small domains with closely related topology.
The gene colipase (CLPS) encodes a lipolytic enzyme that is majorly expressed in the exocrine pancreas. This protein is also found in the stomach and intestine. Its structure includes 17 amino acid signal peptides and a five amino acid pro-piece at the N-terminus.

Application

Colipase from porcine pancreas has been used:

  • in the enzyme solution for lipase assay
  • in an enzyme mixture to simulate gastrointestinal digestion
  • as one of the apparent critical factors to study its effect on lycopene in vitro accessibility

Biochem/physiol Actions

Colipase is involved in lipid metabolism and apoptosis signaling. It is crucial for fat digestion. It is a pancreatic protein that prevents the denaturation of lipase and enables its attachment to the lipid-water interphase of the droplet. Colipase makes lipase accessible to the inner core of triacylglycerol. Defective colipase secretion induced by an insufficient exocrine pancreatic function minimizes the luminal hydrolysis of dietary fat. Lack of congenital lipase or colipase causes pancreatic fat malabsorption.
Colipase, a small protein cofactor, is essential for efficient dietary lipid hydrolysis by pancreatic lipase. It attaches to the non-catalytic C-terminal domain of the lipase, stabilizing an active conformation and significantly enhancing the overall hydrophobic binding site. This pancreatic exocrine protein aids in the adsorption of pancreatic triglyceride lipase (PTL) to the substrate lipid-water interface.

Features and Benefits

  • Overcomes the inhibition of lipase by bile salts.
  • Activity can be demonstrated turbidimetrically in an emulsion of triolein and sodium deoxycholate together with porcine pancreatic lipase.

Preparation Note

Dissolves in water to form a clear, colorless to faint yellow colored solution at 1.9-2.1 mg/mL concentration.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

动植物源性产品

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Certificates of Analysis (COA)

Lot/Batch Number
0000376875
0000328495
0000328495
0000376875
0000240031

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  5. What is the molecular weight of Product C3028, Colipase from porcine pancreas?

    According to Biochim. Biophys. Acta, 271, 400 (1972) the molecular weight of this protein is approximately 10,000 daltons, based on analysis by several techniques (diffusion sedimentation, and gel filtration). A molecular weight of 10,325 daltons has been calculated based on the amino acid composition and amino acid sequence of colipase, which is described in the Journal of Lipid Research, 20, 805-816, (1979).This product is likely to be a mixture of Colipase I and II as described in the following reference: Erlanson, C., et al., Biochim. Biophys. Acta, 310, 437, (1973). This is based on our SDS-PAGE results. The gel pattern shows two major bands, which probably correspond to the two forms of colipases. Minor bands at higher molecular weight may be pro-colipases, or perhaps other unrelated porcine pancreatic proteins.

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W Junge et al.
Clinica chimica acta; international journal of clinical chemistry, 123(3), 293-302 (1982-08-18)
Colipase, like other pancreatic proteins, is liberated into the circulation in acute pancreatitis. Its concentration was measured in serum by a turbidimetric and in urine by a titrimetric method. The principle of both assays is based on the reactivation of
Pancreatic colipase: chemistry and physiology.
B Borgström et al.
Journal of lipid research, 20(7), 805-816 (1979-09-01)
Colipase Stabilizes the Lid Domain of Pancreatic Triglyceride Lipase ast
Lowe, Mark E.
The Journal of Biological Chemistry, 272, 9-12 (1997)
M D Yago et al.
The British journal of nutrition, 78(1), 27-39 (1997-07-01)
The aim of the present study was to investigate in human subjects whether or not the ingestion of two liquid meals that differed only in their fatty acid composition (due to the addition of olive oil (group O) or sunflowerseed
H van Tilbeurgh et al.
Biochimica et biophysica acta, 1441(2-3), 173-184 (1999-11-26)
Colipase is a small protein cofactor needed by pancreatic lipase for the efficient dietary lipid hydrolysis. It binds to the C-terminal, non-catalytic domain of lipase, thereby stabilising an active conformation and considerably increasing the overall hydrophobic binding site. Structural studies
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