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Key Documents

D1315

Sigma-Aldrich

DT Diaphorase (NQO1) human

lyophilized powder, recombinant, expressed in E. coli, ≥90% (SDS-PAGE)

Synonyme(s) :

DTD, NQO1, Quinone reductase

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About This Item

Numéro de classification (Commission des enzymes):
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Produit recombinant

expressed in E. coli

Niveau de qualité

Pureté

≥90% (SDS-PAGE)

Forme

lyophilized powder

Activité spécifique

≥100 units/mg protein

Poids mol.

monomer 31000

Numéro d'accès UniProt

Température de stockage

2-8°C

Informations sur le gène

human ... NQO1(1728)

Application

Human DT diaphorase has been used in a study to assess the development of novel quinone phosphorodiamidate prodrugs. Human DT diaphorase has also been used to investigate its crystal structure for the development of a model for its interaction with the cytotoxic prodrug 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB1954).

Actions biochimiques/physiologiques

DT-diaphorase, also referred to as NAD(P)H:(quinone-acceptor) oxidoreductase, is involved in the reductive activation process of several cytotoxic antitumor quinones and nitrobenzenes. It catalyzes the two-electron reduction of quinones and quinonoid compounds to hydroquinones, using either NADH or NADPH as the electron donor. The flavoenzyme contains one mole of FAD per mole of enzyme.
NQO1 is a cytosolic homodimeric FAD-dependent enzyme that catalyses the reduction of a broad range of cytotoxic quinones resulting in protection from cellular oxidative stress. Oxidative stress may also enhance NQO1-mediated protection of p53 and p73 against proteasomal degredation. The highly Inducible expression of NQO1 is controlled by the Nrf2-Keap1/ARE pathway and appears to be affected by changes in susceptibility to oxidative stress. During Oxygen/glucose deprivation, NQO1 appears to be involved in AMPK-induced cancer cell death. NQO1 has been observed to be overexpressed in several types of solid tumors, including breast, pancreas, lung and colon cancer.
Shown to activate quinone based anti-tumor agents in vivo. Suitable for conjugation to carrier molecules.

Définition de l'unité

One unit will reduce 1.0 μmole cytochrome C per min/mg in the presence of menadione substrate at 37 °C.

Inhibiteur

Réf. du produit
Description
Tarif

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Eeva-Riikka Vehniäinen et al.
Aquatic toxicology (Amsterdam, Netherlands), 116-117, 102-108 (2012-04-10)
Ethoxyresorufin-O-deethylase (EROD) activity is a biomarker of exposure to planar aromatic hydrocarbons, and it is often measured from the S9 fraction. The effect of the liver S9 fraction of seven boreal freshwater fish species on the fluorescence of resorufin was
S Chen et al.
The Journal of biological chemistry, 272(3), 1437-1439 (1997-01-17)
DT-diaphorase (EC 1.6.99.2), also referred to as NAD(P)H:(quinone-acceptor) oxidoreductase, is involved in the reductive activation process of several cytotoxic antitumor quinones and nitrobenzenes. It has been observed in our and other laboratories that the rat enzyme is significantly more effective
C Flader et al.
Journal of medicinal chemistry, 43(16), 3157-3167 (2000-08-24)
A series of naphthoquinone and benzimidazolequinone phosphorodiamidates has been synthesized and studied as potential cytotoxic prodrugs activated by DT-diaphorase. Reduction of the quinone moiety in the target compounds was expected to provide a pathway for expulsion of the phosphoramide mustard
Yang Yang et al.
Journal of experimental & clinical cancer research : CR, 33, 14-14 (2014-02-07)
NAD (P) H: quinone oxidoreductase 1 (NQO1) is a xenobiotic metabolizing enzyme that detoxifies chemical stressors and antioxidants, providing cytoprotection in normal tissues. However, high-level expression of NQO1 has been correlated with numerous human malignancies, suggesting a role in carcinogenesis
David Siegel et al.
Frontiers in pharmacology, 13, 1015642-1015642 (2022-11-22)
The stress induced protein NQO1 can participate in a wide range of biological pathways which are dependent upon the interaction of NQO1 with protein targets. Many of the protein-protein interactions involving NQO1 have been shown to be regulated by the

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