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Key Documents

N9608

Sigma-Aldrich

4′-Nitroacetophenone

98%

Synonym(s):

1-(4-Nitrophenyl)ethan-1-one, 1-(4-Nitrophenyl)ethanone, 1-Acetyl-4-nitrobenzene, 4-Nitrophenyl methyl ketone, 4′-Nitroacetophenone, p-Acetylnitrobenzene

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About This Item

Linear Formula:
O2NC6H4COCH3
CAS Number:
Molecular Weight:
165.15
Beilstein:
607777
EC Number:
MDL number:
UNSPSC Code:
12352100
PubChem Substance ID:
NACRES:
NA.22

Quality Level

Assay

98%

form

crystals

bp

202 °C (lit.)

mp

75-78 °C (lit.)

SMILES string

CC(=O)c1ccc(cc1)[N+]([O-])=O

InChI

1S/C8H7NO3/c1-6(10)7-2-4-8(5-3-7)9(11)12/h2-5H,1H3

InChI key

YQYGPGKTNQNXMH-UHFFFAOYSA-N

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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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Modification of radiation sensitivity of Bacillus megaterium spores by N2O and p-nitroacetophenone.
D Ewing et al.
Radiation research, 58(3), 481-488 (1974-06-01)
Chemical radiosensitization of anoxic mammalian cells: effect of cell concentration.
D A Agnew et al.
Radiation research, 57(2), 246-259 (1974-02-01)
K Tatsumi et al.
Journal of pharmacobio-dynamics, 4(2), 101-108 (1981-02-01)
The electron transfer mechanism in the reduction of aromatic nitro compounds by xanthine oxidase was investigated using methyl p-nitrobenzoate and p-nitroacetophenone as substrates. Methyl p-nitrobenzene was reduced by both one-electron and more than two-electron transfer mechanisms in the enzyme-electron donor
[Semiconservative and unscheduled DNA-synthesis of rat thymocytes under the influence of some radioprotecting and radiosensitizing agents (author's transl)].
K Tempel et al.
Strahlentherapie, 158(2), 112-122 (1982-02-01)
J M Wong et al.
Pharmacogenetics, 3(2), 110-115 (1993-04-01)
The enzyme family carbonyl reductase, which catalyses the reduction of xenobiotic as well as endogenous ketones and aldehydes, has not been very well studied in terms of its biological functions and structural aspects. The aim of the present study was

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