E0887
Esterase from rabbit liver
lyophilized powder, ≥30 units/mg protein
Synonyme(s) :
Carboxyl esterase, Carboxylic-ester hydrolase
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About This Item
Produits recommandés
Forme
lyophilized powder
Niveau de qualité
Activité spécifique
≥30 units/mg protein
Poids mol.
60 kDa
Composition
Protein, ≥85% biuret
Température de stockage
−20°C
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Description générale
Esterase belongs to the C-family of carboxylesterases. It is a glycoprotein, mainly present in the endoplasmic reticulum of hepatocytes.
Application
Esterase from rabbit liver has been used in a study to investigate a toxic effect of carbamate insecticides. Esterase from rabbit liver has also been used in a study to investigate the effect of simvastatin on expression and activity of a lipoprotein-associated phospholipase A(2).
Esterase from rabbit liver has been used:
- in comparative biophysical studies with bovine bile-salt-activated lipase in the assays with vinyl acetate, triacylglycerols, p-nitrophenyl esters and serine enzyme inhibitors
- in the catalysis and kinetic profiling studies of peptidic compounds
- in in vitro stability assays of prodrug compounds (BMS-292655 and BMS300043)
- in the hydrolysis of oleuropein aglycone (Ole-AG)
The enzyme from Sigma has been used to study the effect of divalent metal ions on the activity of esterase.
Actions biochimiques/physiologiques
Esterase enzyme catalyzes hydrolysis of carboxylic ester to carboxylate and alcohol in the presence of water. Rabbit liver carboxylesterase catalyzes enantioselective hydrolysis of cineol derivatives.
Esterase enzyme has broad substrate specificity. Esterase from rabbit liver has been used to investigate the toxic effect of carbamate insecticides. Esterase from rabbit liver has also been used for the hydrolysis of simvastatin.
Définition de l'unité
One unit will hydrolyze 1.0 μmole of ethyl butyrate to butyric acid and ethanol per min at pH 8.0 at 25 °C.
Forme physique
Lyophilized powder containing Tris buffer salts
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
Classification des risques
Resp. Sens. 1
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
Certificats d'analyse (COA)
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Les clients ont également consulté
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Langmuir : the ACS journal of surfaces and colloids, 36(22), 6261-6267 (2020-05-19)
To explore the potential of step-by-step assembly in the fabrication of biological materials, we designed and synthesized two peptide-based molecules for enzyme-instructed hierarchical assembly. Upon the treatment of alkaline phosphatase, one molecule undergoes enzyme-instructed self-assembly forming uniformed nanofibers. The other
Henri Chahinian et al.
Biochimica et biophysica acta, 1801(11), 1195-1204 (2010-07-27)
To differentiate esterases from lipases at the structure-function level, we have compared the kinetic properties and structural features of sequence-related esterase 1 from rabbit liver (rLE) and bile-salt-activated lipase from bovine pancreas (bBAL). In contrast to rLE, bBAL hydrolyses water-insoluble
Anna Sobeková et al.
Acta biologica Hungarica, 60(1), 45-54 (2009-04-22)
The activities of the antioxidant and detoxifying enzymes, superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GSHPx), glutathione reductase (GR), glutathione-S-transferase (GST), and the content of thiobarbituric acid reactive substances (TBARS) were determined in the liver and kidney of rabbits after
Hansjörg Schwertz et al.
Journal of cardiovascular pharmacology, 52(2), 151-160 (2008-08-02)
Animal data strongly support a role for inflammation in myocardial ischemia reperfusion injury. Attempts at cardioprotection by immunomodulation (such as with the specific C5 antibody pexelizumab) in humans have been disappointing. We hypothesized that a broader spectrum antiinflammatory agent might
Z Qiao et al.
The Journal of international medical research, 37(4), 1029-1037 (2009-09-19)
Lipoprotein-associated phospholipase A(2) (Lp-PLA(2)) contributes to atherosclerotic plaque instability and subsequent sudden coronary death. Statins are associated with decreased stroke risk and may improve stability of atherosclerotic plaques. The present study investigated the effect of simvastatin on expression of Lp-PLA(2)
Protocoles
Objective: To standardize a procedure for the enzymatic determination of Esterase activity using Ethyl Butyrate as a substrate.
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