Product Name
Carboxylesterase 2 human, recombinant, expressed in mouse NSO cells, ≥95% (SDS-PAGE)
specific activity
≥1.0 EU/μg
30,000 pmol/min-μg protein
recombinant
expressed in mouse NSO cells
assay
≥95% (SDS-PAGE)
form
solution
mol wt
predicted mol wt ~60 kDa
concentration
0.4-0.6 mg/mL
impurities
≤1.0 EU/μg endotoxin
shipped in
dry ice
storage temp.
−70°C
Quality Level
Gene Information
human ... CES2(8824)
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Biochem/physiol Actions
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.
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.
Other Notes
One unit will cause the hydrolysis of 1 picomole of p-nitrophenylacetate per minute at pH 7.5 at 25 deg C.
Physical form
Supplied as a solution containing sodium chloride, sodium acetate, and 20% glycerol.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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Teruko Imai
Drug metabolism and pharmacokinetics, 21(3), 173-185 (2006-07-22)
Human carboxylesterase 1 (hCE-1, CES1A1, HU1) and carboxylesterase 2 (hCE-2, hiCE, HU3) are a serine esterase involved in both drug metabolism and activation. Although both hCE-1 and hCE-2 are present in several organs, the hydrolase activity of liver and small
Zhe-Yi Hu et al.
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Critical reviews in eukaryotic gene expression, 22(3), 179-187 (2012-11-13)
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