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46058

Sigma-Aldrich

Esterase from porcine liver

lyophilized, powder, slightly beige, ≥50 U/mg

Synonym(s):

Carboxyl esterase, Carboxylic-ester hydrolase, PLE

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About This Item

CAS Number:
9016-18-6
EC Number:
3.1.1.1 (BRENDA, IUBMB)
EC Number:
232-773-7
MDL number:
MFCD00131030
UNSPSC Code:
12352204
NACRES:
NA.54

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biological source

Porcine liver

Quality Level

100

form

lyophilized solid
powder

quality

lyophilized

specific activity

≥50 U/mg

mol wt

Mr ~162000

color

slightly beige

storage temp.

−20°C

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This Item
E0887E2884E3019
Sigma-Aldrich

Sigma-Aldrich

46058

Esterase from porcine liver

Esterase from rabbit liver lyophilized powder, ≥30 units/mg protein

Sigma-Aldrich

E0887

Esterase from rabbit liver

Esterase from porcine liver ammonium sulfate suspension, ≥150 units/mg protein (biuret)

Sigma-Aldrich

E2884

Esterase from porcine liver

Esterase from porcine liver lyophilized powder, ≥15 units/mg solid

Sigma-Aldrich

E3019

Esterase from porcine liver

biological source

Porcine liver

biological source

-

biological source

Porcine liver

biological source

-

specific activity

≥50 U/mg

specific activity

≥30 units/mg protein

specific activity

≥150 units/mg protein (biuret)

specific activity

≥15 units/mg solid

form

lyophilized solid, powder

form

lyophilized powder

form

ammonium sulfate suspension

form

lyophilized powder

mol wt

Mr ~162000

mol wt

60 kDa

mol wt

168 kDa

mol wt

168 kDa

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

−20°C

Quality Level

100

Quality Level

200

Quality Level

300

Quality Level

300

General description

Porcine liver esterase (PLE) is localized in the endoplasmic reticulum (ER).[1]

Application

Esterase from porcine liver has been used as a negative control in fluorescence measurement studies.[2]
Pig liver esterase is commonly used for kinetic resolutions and assymetric synthesis in organic chemistry[3][4].
Porcine liver esterase is used to catalyze the hydrolysis of pentaacetyl catechin and epicatechin for use in pharmaceutical and industrial applications.

Pig liver esterase is commonly used for kinetic resolutions and assymetric synthesis in organic chemistry.

Biochem/physiol Actions

Esterase acts on water-soluble carboxyl esters containing short chain fatty acids. Its functionality is attributed to the catalytic triad of Ser, His and Asp/Glu.
Porcine liver esterase (PLE) displays good stability,[5] broad substrate specificity[1], and is a low-cost enzyme. It is useful in the hydrolysis of ester- and amide-containing compounds, to free acids and is useful detoxification of xenobiotics.[1]

Other Notes

1 U corresponds to the amount of enzyme which hydrolyzes 1 μmol ethyl valerate (CAt. No. 30784) per minute at pH 8.0 and 25°C
contains 1,4-dithioerythritol

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Sales restrictions may apply.

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificates of Analysis (COA)

Lot/Batch Number
BCCD7346
BCCL7924
BCCJ5320
BCCC8217
BCCB1237

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Active-site model for interpreting and predicting the specificity of pig liver esterase
Toone, EJ et al.
Journal of the American Chemical Society, 112, 4946-4952 (1990)
Scale-up of a recombinant pig liver esterase-catalyzed desymmetrization of Dimethyl Cyclohex-4-ene-cis-1, 2-dicarboxylate
Su?ss P, et al.
Organic Process Research & Development, 18 (2014)
Elke Brüsehaber et al.
Bioorganic & medicinal chemistry, 17(23), 7878-7883 (2009-11-04)
The possible physiological role of PLE (E.C. 3.1.1.1) located in the endoplasmic reticulum (ER) of pig liver cells in the conversion of endogenous compounds was investigated as it was reported, that PLE acts as prenylated methylated protein methyl esterase (PMPMEase)
Qing Zhu et al.
Macromolecular rapid communications, 31(12), 1060-1064 (2011-05-19)
Herein we describe a novel and simple conjugated polymer-fluorescent probe based platform for trypsin detection from protein mixtures in homogeneous solution. This platform takes advantage of specific interaction between the probe and the active site of trypsin and the electrostatic
Bornscheuer, UT & Kazlauskas, RJ
Hydrolases in Organic Synthesis, 2 (2005)
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