C3766
Cholesterol Esterase from bovine pancreas
lyophilized powder, ≥200 units/g protein
Sinónimos:
Sterol-ester acylhydrolase
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About This Item
Productos recomendados
form
lyophilized powder
Quality Level
specific activity
≥200 units/g protein
mol wt
84 kDa by SDS-PAGE
composition
protein, ≥20%
storage temp.
−20°C
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General description
Cholesterol Esterase from bovine pancreas is a member of α-β hydrolase superfamily. The core of the protein comprises 11 β-strands, surrounded by 15 α-strands. Catalytic triad is in the centre of the molecule. The C-terminus possesses hydrophobic residues.
Application
Cholesterol Esterase from bovine pancreas has been used:
- in γ-oryzanol-hydrolyzing activity
- in cholesterol esterase enzyme activity for quantification of cholesterol and cholesterol esters associated in tear film and lenses samples
- to test in vitro degradation of poly(fumaroyl bioxirane) maleate (PFM) polymer designed for bone tissue engineering
Cholesterol esterase bound to membrane-associated heparin on brush border membranes aids in the transport of cholesterol and free fatty acid across the membrane. This enzyme is widely used in the determination of serum cholesterol in clinical laboratories. The enzyme from Sigma has been used to evaluate the inhibitory and antioxidant functions of the methanol extract of the Camellia sinensis leaves under in vitro conditions. The enzyme has also been used to digest human serum samples to confirm the presence and position of acyl esters of 7α-hydroxycholesterol.
Enzyme responsible for the hydrolysis of many of the fatty acid esters of cholesterol.
Optimum pH range: 6-8
Activators: Bisphenol A diglycidyl ether, cAMP-dependent protein kinase type II, ethanol, methanol, n-butanol, phosphatidylcholine, phosphatidylethanolamine, sodium taurocholic acid
Inhibitors: Bisphenol A methacrylate, diisopropylfluorophosphate, enolase, Hg2+, sodium fluoride, phosphatidic acid, phosphatidylcholine, phosphatidylserine
Optimum pH range: 6-8
Activators: Bisphenol A diglycidyl ether, cAMP-dependent protein kinase type II, ethanol, methanol, n-butanol, phosphatidylcholine, phosphatidylethanolamine, sodium taurocholic acid
Inhibitors: Bisphenol A methacrylate, diisopropylfluorophosphate, enolase, Hg2+, sodium fluoride, phosphatidic acid, phosphatidylcholine, phosphatidylserine
Biochem/physiol Actions
Cholesterol esterase (CE) is a reversible enzyme that can hydrolyze or synthesize fatty acid esters of cholesterol and other sterols. Hydrolysis of water insoluble long chain fatty acid esters requires bile salt activation. Hydrolysis of water soluble esters of short chain fatty acids and lysophospholipids does not require activation by bile salts. It also hydrolyzes tri-, di-, and mono-acylglycerols, phospholipids, lysophospholipids, and ceramide. This monomeric glycoprotein may have multiple functions in lipid and lipoprotein metabolism, as well as in atherosclerosis. Its molecular mass is found to be 84 kDa.
Other Notes
Partially purified
Unit Definition
One unit will hydrolyze 1.0 μmole of cholesteryl oleate to cholesterol and oleic acid per minute at pH 7.0 at 37 °C in the presence of taurocholate.
Physical form
This product is partially purified from bovine pancreas and is supplied as a white to light brown lyophilized powder containing ≥20% protein (biuret) and potassium phosphate.
Preparation Note
Cholesterol esterase is soluble in 0.4 M potassium phosphate, pH 7.0 at 1 mg/mL concentration.
Analysis Note
Protein determined by biuret.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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H Oda et al.
Journal of lipid research, 31(12), 2209-2218 (1990-12-01)
Serum levels of 7 alpha-hydroxycholesterol and activities of hepatic microsomal cholesterol 7 alpha-hydroxylase in surgical patients were analyzed by capillary gas-liquid chromatography-selected ion monitoring technique using a new internal standard, 5 alpha-cholestane-3 beta, 7 beta-diol. We found that concentrations of
Enzyme-catalyzed hydrolysis of gamma-oryzanol.
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European Food Research and Technology, 218(4), 349-354 (2004)
A Lopez-Candales et al.
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We have recently hypothesized that neutral lipids can, in part, move across biological membranes via a mechanism involving enzymes anchored to membrane proteoglycans such as those found in the brush border of the enterocyte [Bosner, M. S., Gulick, T., Riley
A functional polymer designed for bone tissue engineering.
You Z, et al.
Acta Biomaterialia, 8(2), 502-510 (2012)
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