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Merck
CN

61716

4-Nitrophenyl dodecanoate

≥98.0% (GC)

Synonym(s):

4-Nitrophenyl laurate, Dodecanoic acid 4-nitrophenyl ester

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About This Item

Empirical Formula (Hill Notation):
C18H27NO4
CAS Number:
1956-11-2
Molecular Weight:
321.41
UNSPSC Code:
12352204
NACRES:
NA.83
PubChem Substance ID:
57651858
EC Number:
217-796-2
Beilstein/REAXYS Number:
1889084
MDL number:
MFCD00047730

Key Documents

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Product Name

4-Nitrophenyl dodecanoate, ≥98.0% (GC)

InChI key

YNGNVZFHHJEZKD-UHFFFAOYSA-N

InChI

1S/C18H27NO4/c1-2-3-4-5-6-7-8-9-10-11-18(20)23-17-14-12-16(13-15-17)19(21)22/h12-15H,2-11H2,1H3

SMILES string

CCCCCCCCCCCC(=O)Oc1ccc(cc1)[N+]([O-])=O

assay

≥98.0% (GC)

mp

~46 °C

solubility

chloroform: 1 g/10 mL, clear, colorless to faintly greenish-yellow

storage temp.

2-8°C

Quality Level

100

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Application

4-Nitrophenyl dodecanoate has been used as a substrate:
  • for carboxylesterase to assess the enzyme-substrate affinity
  • in a chromogenic assay to evaluate lipase activity
  • to determine the esterase activity of patatin

Biochem/physiol Actions

4-Nitrophenyl dodecanoate is a p-nitrophenol ester derivative and serves as a typical model substrate in lipase assays.

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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Certificates of Analysis (COA)

Lot/Batch Number
BCCP0488
BCCK8091
BCCH0632
BCCD5633
BCCB0264

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T L R Corrêa et al.
Journal of applied microbiology, 115(1), 114-124 (2013-04-16)
In this study, a gene that encodes a carboxylesterase (carb) in Penicillium expansum GF was cloned, sequenced and overexpressed by Penicillium griseoroseum PG63, and the enzyme was characterized. The recombinant strain, P. griseoroseum T55, obtained upon transformation using the plasmid
P Fuciños et al.
Journal of biotechnology, 117(3), 233-241 (2005-05-03)
Thermus thermophilus HB27 produces important levels of extracellular lipolytic activity when grown for 30 h at 70 degrees C in a complex medium. A method to detect esterase activity in these samples after non-reducing SDS-polyacrylamide electrophoresis was developed. The method
Chemical characterization and functional properties of a potato protein concentrate prepared by large-scale expanded bed adsorption chromatography
Lokra S, et al.
LWT--Food Science and Technology, 1089-1099 null
Crosslinked, biodegradable polyurethanes for precision-porous biomaterials: synthesis and properties
Calleros EL, et al.
Journal of Applied Polymer Science, 48943 null
K Itoyama et al.
Biotechnology progress, 10(2), 225-229 (1994-03-01)
Lipoprotein lipase (LPL) was covalently immobilized onto the surface of porous chitosan beads (ChB) without or with spacers of different lengths. The relative activity (RA) of the immobilized LPL was found to be high toward a small ester substrate, p-nitrophenyl
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