NQO2 Human

NAD(P)H Dehydrogenase Quinone 2 Human Recombinant
Cat. No.
BT13949
Source
Escherichia Coli.
Synonyms
DHQV, DIA6, QR2, EC 1.10.99.2, NMOR2, NQO2, NRH:quinone oxidoreductase 2, NRH dehydrogenase [quinone] 2, Ribosyldihydronicotinamide dehydrogenase [quinone].
Appearance
Sterile filtered colorless solution.
Purity
Greater than 95% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

NQO2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 251amino acids (1-231 a.a.) and having a molecular mass of 28.1 kDa. NQO2 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.

Product Specs

Introduction
NQO2, a flavoprotein, plays a crucial role in the two-electron reduction of various molecules, including quinones, redox dyes, and vitamin K menadione. It primarily utilizes dihydronicotinamide riboside (NRH) as an electron donor. NQO2's significance lies in its ability to catalyze the detoxification of quinones and their derivatives by converting them into hydroquinones. This detoxification process is essential for protecting cells from oxidative stress, cytotoxicity, and mutagenicity induced by quinones.
Description
Recombinant human NQO2, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 251 amino acids (specifically, amino acids 1 to 231) and possessing a molecular weight of 28.1 kDa. This protein is engineered with a 20 amino acid His-Tag fused to its N-terminus to facilitate purification through standard chromatographic techniques.
Physical Appearance
The product is a sterile, colorless solution that has been filtered for sterility.
Formulation
This solution contains human NQO2 at a concentration of 1 mg/ml. It is formulated in a buffer consisting of 20mM Tris-HCl at pH 8, 1mM DTT, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. To ensure optimal stability during long-term storage, consider adding a carrier protein such as HSA or BSA at a concentration of 0.1%. It is crucial to minimize repeated freeze-thaw cycles to maintain product integrity.
Purity
The purity of this product is greater than 95%, as assessed by SDS-PAGE analysis.
Synonyms
DHQV, DIA6, QR2, EC 1.10.99.2, NMOR2, NQO2, NRH:quinone oxidoreductase 2, NRH dehydrogenase [quinone] 2, Ribosyldihydronicotinamide dehydrogenase [quinone].
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAGKKVLIVY AHQEPKSFNG SLKNVAVDEL SRQGCTVTVS DLYAMNFEPR ATDKDITGTL SNPEVFNYGV ETHEAYKQRS LASDITDEQK KVREADLVIF QFPLYWFSVP AILKGWMDRV LCQGFAFDIP GFYDSGLLQG KLALLSVTTG GTAEMYTKTG VNGDSRYFLW PLQHGTLHFC GFKVLAPQIS FAPEIASEEE RKGMVAAWSQ RLQTIWKEEP IPCTAHWHFG Q.

Product Science Overview

Structure and Mechanism

NQO2 is a cytosolic flavoprotein that functions as a homodimer . It contains two catalytic flavin adenine dinucleotide (FAD) cofactors and two zinc ions, although the role of zinc in its catalytic activity is not fully understood . The enzyme operates through a ping-pong mechanism involving its FAD cofactor . In the reductive phase, NQO2 binds to reduced dihydronicotinamide riboside (NRH) as an electron donor and mediates a hydride transfer from NRH to FAD. In the oxidative phase, NQO2 binds to its quinone substrate and reduces it to a dihydroquinone .

Function and Importance

NQO2 is a phase II detoxification enzyme that can carry out two or four electron reductions of quinones . This detoxification process is essential as it protects cells against quinone-induced oxidative stress, cytotoxicity, and mutagenicity . Quinones are potentially dangerous because they can undergo one-electron reduction to form semiquinones, which elicit oxidative stress in cells . By reducing quinones to hydroquinones through a two-electron step, NQO2 prevents the formation of reactive oxygen species .

Clinical Relevance

NQO2 has been found to be overexpressed in certain types of tumors and is upregulated as part of the oxidative stress response . It also has a melatonin-binding site, which may explain the antioxidant role of melatonin . Interestingly, NQO2 can be inhibited by resveratrol, a compound found in red wine .

Evolutionary Perspective

The NQO gene family is ancient, believed to be between 2 and more than 3 billion years old . This family includes NQO1 and NQO2 in humans, and these genes encode enzymes that catalyze the beneficial two-electron reduction of quinones to hydroquinones . This evolutionary development likely provided a significant advantage by protecting early organisms from oxidative damage caused by quinones .

Applications

Recombinant NQO2 is used in various research applications to study its role in detoxification, oxidative stress response, and its potential involvement in cancer and other diseases . Understanding the function and regulation of NQO2 can provide insights into developing therapeutic strategies for conditions associated with oxidative stress and quinone toxicity.

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