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62314

Sigma-Aldrich

Lipase Substrate

for the titrimetric determination of enzyme activity

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About This Item

UNSPSC Code:
12352204
NACRES:
NA.32

grade

for the titrimetric determination of enzyme activity

Quality Level

form

liquid

technique(s)

titration: suitable

refractive index

n20/D 1.36

density

1.05 g/mL at 20 °C

storage temp.

2-8°C

Physical form

aqueous solution with 4.5 mM triolein; 1 M NaCl; 13% (w/v) Triton X-100

Other Notes

Assay of microbial lipases with emulsified trioleoyl glycerol; the fatty acids released are titrated with a pH stat

Legal Information

Triton is a trademark of The Dow Chemical Company or an affiliated company of Dow

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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A new assay of microbial lipases with emulsified trioleoyl glycerol.
N Peled et al.
Analytical biochemistry, 112(2), 219-222 (1981-04-01)
H Schmidinger et al.
Amino acids, 30(4), 333-350 (2006-06-15)
In the postgenomic era new technologies are emerging for global analysis of protein function. The introduction of active site-directed chemical probes for enzymatic activity profiling in complex mixtures, known as activity-based proteomics has greatly accelerated functional annotation of proteins. Here
Hannes Schmidinger et al.
Chembiochem : a European journal of chemical biology, 7(3), 527-534 (2006-02-14)
Protein and small-molecule microarrays are useful tools for high-throughput analysis of DNA-protein, protein-protein, and protein-small molecule interactions. Here we report on novel microarrays for activity screening of lipases and esterases based on phosphonic acid ester inhibitors. These compounds are activity
H Scholze et al.
Analytical biochemistry, 276(1), 72-80 (1999-12-10)
We report on the determination of active enzyme components in pure and crude lipases, using fluorescent inhibitors for covalent modification and visualization of the enzymatically active proteins. Lipase-specific compounds are triacylglycerol analogs, namely 1,2(2, 3)-di-O-alkylglyceroalkylphosphonic acid-p-nitrophenyl esters, containing a fluorescent
Maximilian Schicher et al.
Methods in molecular biology (Clifton, N.J.), 579, 497-511 (2009-09-19)
Lipases are responsible for the hydrolysis of acylglycerols and cholesteryl esters in animals, plants, and microorganisms. In this chapter we describe a tool for the concomitant analysis of lipases in complex proteomes. For this purpose, the target enzymes are selectively

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