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46021

Sigma-Aldrich

4-Nitrophenyl acetate

≥99.0% (GC)

Synonym(s):

Acetic acid 4-nitrophenyl ester

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About This Item

Linear Formula:
CH3CO2C6H4NO2
CAS Number:
Molecular Weight:
181.15
Beilstein:
515874
EC Number:
MDL number:
UNSPSC Code:
12352204
PubChem Substance ID:

Assay

≥99.0% (GC)

form

powder or crystals

mp

75-77 °C (lit.)
77-79 °C

storage temp.

−20°C

SMILES string

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

InChI

1S/C8H7NO4/c1-6(10)13-8-4-2-7(3-5-8)9(11)12/h2-5H,1H3

InChI key

QAUUDNIGJSLPSX-UHFFFAOYSA-N

Gene Information

human ... PON1(5444)

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Other Notes

Activated acetate; reagent for acetylations. Substrate for carboxy-esterase; Substrate for the determination of lipase

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Signal Word

Danger

Hazard Statements

Hazard Classifications

Eye Dam. 1 - Ox. Sol. 3 - Skin Sens. 1

Storage Class Code

5.1B - Oxidizing hazardous materials

WGK

WGK 3

Flash Point(F)

No data available

Flash Point(C)

No data available

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

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C S Wang
The Journal of biological chemistry, 256(19), 10198-10202 (1981-10-10)
Further studies on human milk bile salt-activated lipase were performed to provide kinetic and additional chemical characterizations of this enzyme. The enzyme was homogeneous by urea-sodium dodecyl sulfate-polyacrylamide gel electrophoresis and isoelectric focusing with an isoelectric point of 3.7. A
Multiple forms of carboxylesterases in Baker's yeast.
E Parkkinen
Cellular and molecular biology, including cyto-enzymology, 26(2), 147-154 (1980-01-01)
Hanna Gustafsson et al.
Colloids and surfaces. B, Biointerfaces, 100, 22-30 (2012-07-04)
Immobilization of enzymes usually improves the recyclability and stability and can sometimes also improve the activity compared to enzymes free in solution. Mesoporous silica is a widely studied material as host for immobilized enzymes because of its large internal surface
Conformer selection and intensified dynamics during catalytic turnover in chymotrypsin.
Peter Liuni et al.
Angewandte Chemie (International ed. in English), 51(38), 9666-9669 (2012-09-01)
Arna Runarsdottir et al.
Journal of molecular biology, 401(3), 451-464 (2010-07-06)
Glutathione transferases (GSTs) are known as promiscuous enzymes capable of catalyzing the conjugation of glutathione with a broad range of electrophilic substrates. A previous study based on recombinant chimeras derived from human GST M1-1 and GST M2-2 demonstrated the formation

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