C3028
Colipase from porcine pancreas
essentially salt-free, lyophilized powder
Synonym(s):
Colipase from hog pancreas
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About This Item
biological source
Porcine pancreas
Quality Level
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.
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.
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
Certificates of Analysis (COA)
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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)
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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