Recombinant Human Quinone oxidoreductase protein - BSA and Azide free is a Human Full Length protein, in the 1 to 329 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, MS.
M G S S H H H H H H S S G L V P R G S H M G S M A T G Q K L M R A V R V F E F G G P E V L K L R S D I A V P I P K D H Q V L I K V H A C G V N P V E T Y I R S G T Y S R K P L L P Y T P G S D V A G V I E A V G D N A S A F K K G D R V F T S S T I S G G Y A E Y A L A A D H T V Y K L P E K L D F K Q G A A I G I P Y F T A Y R A L I H S A C V K A G E S V L V H G S G G V G L A A C Q I A R A Y G L K I L G T A G T E E G Q K I V L Q N G A H E V F N H R E V N Y I D K I K K Y V G E K G I D I I I E M L A N V N L S K D L S L L S H G G R V I V V G S R G T I E I N P R D T M A K E S S I I G V T L F S S T K E E F Q Q Y A A A L Q A G M E I G W L K P V I G S Q Y P L E K V A E A H E N I I H G S G A T G K M I L L L
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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Does not have alcohol dehydrogenase activity. Binds NADP and acts through a one-electron transfer process. Orthoquinones, such as 1,2-naphthoquinone or 9,10-phenanthrenequinone, are the best substrates (in vitro). May act in the detoxification of xenobiotics. Interacts with (AU)-rich elements (ARE) in the 3'-UTR of target mRNA species. Enhances the stability of mRNA coding for BCL2. NADPH binding interferes with mRNA binding.
Quinone oxidoreductase, NADPH:quinone reductase, Zeta-crystallin, CRYZ
Recombinant Human Quinone oxidoreductase protein - BSA and Azide free is a Human Full Length protein, in the 1 to 329 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, MS.
pH: 8
Constituents: 20% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab180303 was purified by using conventional chromatography techniques.
Does not have alcohol dehydrogenase activity. Binds NADP and acts through a one-electron transfer process. Orthoquinones, such as 1,2-naphthoquinone or 9,10-phenanthrenequinone, are the best substrates (in vitro). May act in the detoxification of xenobiotics. Interacts with (AU)-rich elements (ARE) in the 3'-UTR of target mRNA species. Enhances the stability of mRNA coding for BCL2. NADPH binding interferes with mRNA binding.
Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.
This product was previously labelled as CRYZ
Quinone oxidoreductase also known by its popular alternate name NQO1 is a flavoenzyme with a molecular mass of approximately 31 kDa. It functions mechanically by catalyzing the reduction of quinones to hydroquinones utilizing NAD(P)H as an electron donor. This enzymatic activity helps in preventing redox cycling and oxidative stress by removing reactive quinones. Quinone oxidoreductase is expressed in various tissues including liver lung and heart highlighting its role in many biological processes.
Quinone oxidoreductase acts as a detoxifying enzyme. It maintains cellular protection against oxidative damage by neutralizing harmful quinones. This enzyme is not reported as part of a larger protein complex but it plays a complementary role with other phase II detoxification enzymes like glutathione S-transferase. Its protective attributes attribute to cell survival especially under oxidative stress conditions.
Quinone oxidoreductase is integral to the oxidative stress response and xenobiotic metabolism pathways. It is closely related to proteins such as cytochrome P450 and glutathione which work together to maintain cellular redox homeostasis and metabolism of foreign compounds. This collaboration allows quinone oxidoreductase to help in converting toxic substances into less harmful forms.
Quinone oxidoreductase is implicated in cancer and neurodegenerative disorders. In cancer its overexpression can lead to chemoresistance as its detoxifying functions may neutralize chemotherapeutic agents sharing functional pathways with proteins like p53. In neurodegenerative diseases altered activity of quinone oxidoreductase influences oxidative damage a common cause in disorders such as Parkinson's disease. Its relation with proteins like PARK7 (DJ-1) highlights its role in protecting neuronal cells from oxidative stress.
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15% SDS-PAGE analysis of ab180303 (3 μg).
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