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Lipase-A Recombinant ( Lipase A )

DescriptionRecombinant Immobilized Serratia marcescens Lipase-A is expressed in E.Coli having a Mw of 65 kDa is purified by standard chromatography techniques.SourceEscherichia Coli.Physical AppearanceSterile Filtered lyophilized

$193.00

Data sheet

Formulation The protein was lyophilized without additives.
Solubility It is recommended to reconstitute the lyophilized Lipase-A in sterile 10%-50% DMSO, isopropyl ether, petroleum ether, ethanol, acetone and isopropanol.
Purity Greater than 90% as determined by SDS-PAGE.
Description Recombinant Immobilized Serratia marcescens Lipase-A is expressed in E.Coli having a Mw of 65 kDa is purified by standard chromatography techniques.
Protein Background Lipase (EC 3.1.1.3) is a ubiquitous enzyme that catalyzes the hydrolysis of fats and oil. The Serratia marcescens lipase is recognized for its excellent enantioselectivity in biocatalytic hydrolysis of trans-3-(4-methoxyphynyl) glycidic acid methyl ester [()-MPGM] to produce (2R, 3S)-3-(4-methoxyphenyl) glycidic acid methyl ester [(-)-MPGM], an important intermediate for the synthesis of diltiazem hydrochlorid.
Expression host Escherichia Coli.
Reagent Appearance Sterile Filtered lyophilized powder.
Stability Recombinant Lipase-A although stable at room temp for 1 week, should be stored desiccated below -18C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Unit Definition Lipase-A was assayed using p-nitrophenyl acetate ( pNPA) as a substrate. One unit of lipase activity was defined as the amount of enzyme releasing 1.0 mol of p-nitrophenol per minute.
Biological Activity 580 units/mg powder.

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