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Carboxylesterase 2 from Human, Recombinant

Cat No.
NATE-0812
Description
Member of a serine esterase family that hydrolyze ester and amide bonds. Carboxylesterase 2 is an endoplasmic reticulum-bound hydrolase that plays a critical role in xenobiotic detoxification and activation for ester-containing therapeutics. Carboxylesterase 2 is also involved in the detoxification of drugs such as heroin and cocaine. This enzyme is thought to play a role in lipid metabolism. Human carboxylesterase 2 (hCE-2) recognizes a substrate with a large alcohol group and small acyl group. Its substrate specificity may be restricted by a capability of acyl-hCE-2 conjugate formation due to the presence of conformational interference in the active site pocket. Carboxylesterases catalyze the biotransformation of several ester-containing drugs and prodrugs such as angiotensin-converting enzyme inhibitor (temocarpil, cilazapril), anti-tumor drugs (capecitabin) and narcotics.
Abbr
CES2, Recombinant (Human)
Alias
CES2; CE-2; CES2A1; PCE-2; Ice
Source
Mouse NSO cells
Species
Human
Form
Supplied as a solution containing sodium chloride, sodium acetate, and 20% glycerol.
Enzyme Commission Number
EC 3.1.1.1
Activity
>30,000 (pmol/min/μg)
CAS No.
9016-18-6
Molecular Weight
~60 kDa
Purity
>95% (SDS-PAGE)
Concentration
0.4 - 0.6 mg/ml
Storage
Store at -70°C
Synonyms
EC 3.1.1.1; Carboxylesterase 2; CES2; CES2A1; CE-2; PCE-2; iCE

"Esterase" Total Products Page

Catalog Product Name EC No. CAS No. Source Price
NATE-1916 Carboxylesterase 1 isoform c from Human, Recombinant EC 3.1.1.1 9016-18-6 Baculovirus infected BTI insect cells Inquiry
NATE-1915 Carboxylesterase 1 isoform b from Human, Recombinant EC 3.1.1.1 9016-18-6 Baculovirus infected BTI insect cells Inquiry
NATE-1633 Carboxylesterase 1D from Mouse, Recombinant Insect cell (Baculovirus) and fused to His-tag at N-terminus Inquiry
NATE-0229 Esterase Isoenzyme 1 from Porcine liver, Recombinant EC 3.1.1.1 9016-18-6 E. coli Inquiry

Our Products Cannot Be Used As Medicines Directly For Personal Use.

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