C3028
Colipase from porcine pancreas
essentially salt-free, lyophilized powder
Synonyme(s) :
Colipase from hog pancreas
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About This Item
Numéro CAS:
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54
Produits recommandés
Source biologique
Porcine pancreas
Niveau de qualité
Pureté
≥95% (Lowry)
Forme
essentially salt-free, lyophilized powder
Concentration
≥500 μ protein/vial
Couleur
white to faint yellow
Solubilité
H2O: soluble 1.9-2.1 mg/mL, clear, colorless to faintly yellow
Adéquation
suitable for molecular biology
Numéro d'accès UniProt
Application(s)
food and beverages
Température de stockage
−20°C
Informations sur le gène
pig ... CLPS(397407)
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Description générale
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.
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
Actions biochimiques/physiologiques
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.
Caractéristiques et avantages
- 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.
Notes préparatoires
Dissolves in water to form a clear, colorless to faint yellow colored solution at 1.9-2.1 mg/mL concentration.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
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Les clients ont également consulté
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
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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