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C3028

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Colipase from porcine pancreas

essentially salt-free, lyophilized powder

Sinónimos:

Colipase from hog pancreas

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About This Item

Número de CAS:
Número CE:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54

origen biológico

Porcine pancreas

Nivel de calidad

Ensayo

≥95% (Lowry)

Formulario

essentially salt-free, lyophilized powder

concentración

≥500 μ protein/vial

color

white to faint yellow

solubilidad

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

idoneidad

suitable for molecular biology

Nº de acceso UniProt

aplicaciones

food and beverages

temp. de almacenamiento

−20°C

Información sobre el gen

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Descripción general

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.

Aplicación

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

Acciones bioquímicas o fisiológicas

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.

Características y beneficios

  • 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.

Nota de preparación

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

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

Eyeshields, Gloves, type N95 (US)


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Colipase Stabilizes the Lid Domain of Pancreatic Triglyceride Lipase ast
Lowe, Mark E.
The Journal of Biological Chemistry, 272, 9-12 (1997)
Pancreatic colipase: chemistry and physiology.
B Borgström et al.
Journal of lipid research, 20(7), 805-816 (1979-09-01)
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
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
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

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