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D7816

Sigma-Aldrich

1,2-Di-O-lauryl-rac-glycero-3-glutaric acid 6′-methylresorufin ester

lipase substrate, solid

Synonym(s):

Chromogenic lipase substrate

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About This Item

UNSPSC Code:
12352204
PubChem Substance ID:
329798787
NACRES:
NA.32

product name

1,2-Di-O-lauryl-rac-glycero-3-glutaric acid 6′-methylresorufin ester, lipase substrate

form

solid

storage temp.

2-8°C

SMILES string

CCCCCCCCCCCCOCC(COC(=O)CCCC(=O)Oc1ccc2N=C3C=CC(=O)C=C3Oc2c1C)OCCCCCCCCCCCC

InChI

1S/C45H69NO8/c1-4-6-8-10-12-14-16-18-20-22-31-50-34-38(51-32-23-21-19-17-15-13-11-9-7-5-2)35-52-43(48)25-24-26-44(49)53-41-30-29-40-45(36(41)3)54-42-33-37(47)27-28-39(42)46-40/h27-30,33,38H,4-26,31-32,34-35H2,1-3H3

InChI key

JEGLJLCZRAWOBI-UHFFFAOYSA-N

Application

Chromogenic substrate for lipase

Biochem/physiol Actions

1,2-Di-O-lauryl-rac-glycero-3-glutaric acid 6′-methylresorufin ester (DGGR) is more pancreas-specific. Hence the DGGR lipase assay may be preferred as a substitute to spec cPL in diagnostic cases with suspected pancreatitis.

Storage Class Code

11 - Combustible Solids

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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Validation of a commercial 1, 2-o-dilauryl-rac-glycero glutaric acid-(6?-methylresorufin) ester lipase assay for diagnosis of canine pancreatitis
Goodband E L, et al.
Veterinary record open, 5(1), e000270-e000270 (2018)
Narmadaa Thyagarajan et al.
Lipids, 52(3), 189-205 (2017-02-17)
Macrophage lipoprotein lipase (LPL) induces lipid accumulation and promotes atherosclerosis. However, the effects of lipoprotein hydrolysis products generated by LPL on macrophage-derived foam cell formation are not clearly understood. Thus, we analyzed the transcriptomic response to hydrolysis products via microarray
Breanne M Coady et al.
Journal of peptide science : an official publication of the European Peptide Society, 24(11), e3123-e3123 (2018-10-06)
Human hepatic lipase (hHL) is a cell surface associated enzyme that hydrolyzes triacylglycerols and phospholipids within circulating lipoproteins. We hypothesized that an amino acid sequence mimicking the major heparin binding domain (HBD) of hHL will displace hHL from cell surfaces.

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