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E0162

Sigma-Aldrich

Carboxylesterase 1 isoform c human

recombinant, expressed in baculovirus infected BTI insect cells

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Synonym(s):
Carboxylesterase 1 human, carboxylesterase, esterase
Enzyme Commission number:
3.1.1.1 (BRENDA, IUBMB)
EC Number:
232-773-7
NACRES:
NA.54

recombinant

expressed in baculovirus infected BTI insect cells

Quality Level

200

form

liquid

concentration

≥0.3 mg/mL

shipped in

dry ice

storage temp.

−70°C

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General description

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

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. It has also been used as a commercial recombinant protein for the methodological validation of environmental chemical-based inhibition studies.

Biochem/physiol Actions

Carboxylesterase enzymes are responsible for the hydrolysis of ester- and amide-bond-containing drugs such as cocaine and heroin. 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). It also hydrolyzes aromatic and aliphatic esters with preference to small alcohol groups and bulky acyl groups. CE1 metabolizes drug esters and amides carbamates. It participates in the detoxification of environmental toxicants and carcinogens and is useful in pharmacokinetic studies for evaluating pro-drugs.

Physical properties

This product is offered in a volume of 0.5 mL.

Unit Definition

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

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

常规特殊物品

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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)
Plasmatic B-esterases as potential biomarkers of exposure to marine plastics in loggerhead turtles.
Sole, et al.
Environmental Research, 213, 113639-113639 (2022)
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
Dandan Wang et al.
Acta pharmaceutica Sinica. B, 8(5), 699-712 (2018-09-25)
Mammalian carboxylesterases (CEs) are key enzymes from the serine hydrolase superfamily. In the human body, two predominant carboxylesterases (CES1 and CES2) have been identified and extensively studied over the past decade. These two enzymes play crucial roles in the metabolism
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