46058
Esterase from porcine liver
lyophilized, powder, slightly beige, ≥50 U/mg
Synonym(s):
Carboxyl esterase, Carboxylic-ester hydrolase, PLE
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$137.00
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Available to ship onApril 28, 2025Details
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10 MG
$137.00
50 MG
$440.85
About This Item
$137.00
Available to ship onApril 28, 2025Details
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biological source
Porcine liver
Quality Level
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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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.
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.
Components
contains 1,4-dithioerythritol
Unit Definition
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
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signalword
Danger
hcodes
pcodes
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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Scale-up of a recombinant pig liver esterase-catalyzed desymmetrization of Dimethyl Cyclohex-4-ene-cis-1, 2-dicarboxylate
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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)
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)
Bornscheuer, UT & Kazlauskas, RJ
Hydrolases in Organic Synthesis, 2 (2005)
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