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D7816

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

Name: 1,2-Di-O-lauryl-<I>rac</I>-glycero-3-glutaric acid 6&#8242;-methylresorufin ester
Brand: SIGMA

lipase substrate, solid

Synonym(s):

Chromogenic lipase substrate

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About This Item

MDL number:

MFCD34471683

UNSPSC Code:

12352204

PubChem Substance ID:

329798787

NACRES:

NA.32

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Product Name

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

Quality Level

200

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

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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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)

Transcriptomic Analysis of THP-1 Macrophages Exposed to Lipoprotein Hydrolysis Products Generated by Lipoprotein Lipase.

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

Characterization of a peptide containing the major heparin binding domain of human hepatic lipase.

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.

Global Trade Item Number

SKU	GTIN
D7816-10MG	04061832923840

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