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E0162

Sigma-Aldrich

Carboxylesterase 1 isoform c human

recombinant, expressed in baculovirus infected BTI insect cells

Synonyme(s) :

Carboxylesterase 1 human, carboxylesterase, esterase

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About This Item

Numéro de classification (Commission des enzymes):
Numéro CE :
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

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Produit recombinant

expressed in baculovirus infected BTI insect cells

Niveau de qualité

Forme

liquid

Concentration

≥0.3 mg/mL

Conditions d'expédition

dry ice

Température de stockage

−70°C

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Description générale

Carboxylesterase 1 (CE1) is a member of a large multigene[1] carboxylesterase α,β-hydrolase family.[2] It is majorly expressed in the liver.[2] CE1 comprises an αβ domain, a central catalytic domain and a regulatory domain.[2]

Application

Carboxylesterase 1 isoform c human has been used as a reference standard in carboxylesterase activity from the mussel for comparison of substrate specificity and inhibition studies.[3] It has also been used as a commercial recombinant protein for the methodological validation of environmental chemical-based inhibition studies.[4]

Actions biochimiques/physiologiques

Carboxylesterase enzymes are responsible for the hydrolysis of ester- and amide-bond-containing drugs such as cocaine and heroin.[2] They also hydrolyze long-chain fatty acid esters and thioesters. Carboxylesterase 1 (CE1) catalyzes the formation of cholesteryl esters from cholesterol and fatty acids. Through a transesterification reaction, CE1 also mediates the generation of fatty acid ethyl esters (FAEEs).[2] It also hydrolyzes aromatic and aliphatic esters[5] with preference to small alcohol groups and bulky acyl groups.[6] CE1 metabolizes drug esters and amides carbamates.[5] It participates in the detoxification of environmental toxicants and carcinogens and is useful in pharmacokinetic studies for evaluating pro-drugs.[7]

Propriétés physiques

This product is offered in a volume of 0.5 mL.

Définition de l'unité

One unit will hydrolyze one nanomole of 4-nitrophenyl acetate per minute at pH 7.4 at 37 °C.

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

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


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Consulter la Bibliothèque de documents

Jihong Lian et al.
Protein & cell, 9(2), 178-195 (2017-07-06)
Mammalian carboxylesterases hydrolyze a wide range of xenobiotic and endogenous compounds, including lipid esters. Physiological functions of carboxylesterases in lipid metabolism and energy homeostasis in vivo have been demonstrated by genetic manipulations and chemical inhibition in mice, and in vitro
Carboxylesterases: sources, characterization and broader applications
Sood S, et al.
Insight (American Society of Ophthalmic Registered Nurses), 1, 1-11 (2016)
S Casey Laizure et al.
Pharmacotherapy, 33(2), 210-222 (2013-02-07)
Carboxylesterases are a multigene family of mammalian enzymes widely distributed throughout the body that catalyze the hydrolysis of esters, amides, thioesters, and carbamates. In humans, two carboxylesterases, hCE1 and hCE2, are important mediators of drug metabolism. Both are expressed in
Plasmatic B-esterases as potential biomarkers of exposure to marine plastics in loggerhead turtles.
Sole, et al.
Environmental Research, 213, 113639-113639 (2022)
Masakiyo Hosokawa
Molecules (Basel, Switzerland), 13(2), 412-431 (2008-02-29)
Mammalian carboxylesterases (CESs) comprise a multigene family whose gene products play important roles in biotransformation of ester- or amide-type prodrugs. They are members of an alpha,beta-hydrolase-fold family and are found in various mammals. It has been suggested that CESs can

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