Carboxylesterase 1 isoform c human

recombinant, expressed in baculovirus infected BTI insect cells

Carboxylesterase 1 human, esterase, carboxylesterase
Enzyme Commission number:
EC Number:

Quality Level


expressed in baculovirus infected BTI insect cells



specific activity

≥1000 units/mg protein


5 mg/mL

shipped in

dry ice

storage temp.


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.


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.


Health hazard

Signal Word


Hazard Statements


NONH for all modes of transport

WGK Germany


Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Certificate of Origin

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...
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)
Montserrat Solé et al.
Environmental toxicology and pharmacology, 82, 103561-103561 (2020-12-12)
Carboxylesterases (CEs) are key enzymes which catalyse the hydrolysis reactions of multiple xenobiotics and endogenous ester moieties. Given their growing interest in the context of marine pollution and biomonitoring, this study focused on the in vitro sensitivity of marine invertebrate...
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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