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Mouse Anti-NQO1 Recombinant Antibody (CBWJN-0685) (CBMAB-N3303-WJ)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBWJN-0685
Application
WB, IF

Basic Information

Specificity
Human
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
NAD(P)H Quinone Dehydrogenase 1
Introduction
This gene is a member of the NAD(P)H dehydrogenase (quinone) family and encodes a cytoplasmic 2-electron reductase. This FAD-binding protein forms homodimers and reduces quinones to hydroquinones. This protein's enzymatic activity prevents the one electron reduction of quinones that results in the production of radical species. Mutations in this gene have been associated with tardive dyskinesia (TD), an increased risk of hematotoxicity after exposure to benzene, and susceptibility to various forms of cancer. Altered expression of this protein has been seen in many tumors and is also associated with Alzheimer's disease (AD). Alternate transcriptional splice variants, encoding different isoforms, have been characterized. [provided by RefSeq, Jul 2008]
Entrez Gene ID
1728
UniProt ID
P15559
Alternative Names
NAD(P)H Quinone Dehydrogenase 1; Diaphorase (NADH/NADPH) (Cytochrome B-5 Reductase); NAD(P)H Dehydrogenase, Quinone 1; NAD(P)H:Quinone Oxidoreductase 1; Phylloquinone Reductase; Menadione Reductase; Quinone Reductase 1; DT-Diaphorase; Azoreductase; EC 1.6.5.2; NMOR1; DIA4;
Function
Flavin-containing quinone reductase that catalyzes two-electron reduction of quinones to hydroquinones using either NADH or NADPH as electron donors. In a ping-pong kinetic mechanism, the electrons are sequentially transferred from NAD(P)H to flavin cofactor and then from reduced flavin to the quinone, bypassing the formation of semiquinone and reactive oxygen species (PubMed:8999809, PubMed:9271353) (By similarity).
Regulates cellular redox state primarily through quinone detoxification. Reduces components of plasma membrane redox system such as coenzyme Q and vitamin quinones, producing antioxidant hydroquinone forms. In the process may function as superoxide scavenger to prevent hydroquinone oxidation and facilitate excretion (PubMed:8999809, PubMed:9271353, PubMed:15102952).
Alternatively, can activate quinones and their derivatives by generating redox reactive hydroquinones with DNA cross-linking antitumor potential (PubMed:8999809).
Acts as a gatekeeper of the core 20S proteasome known to degrade proteins with unstructured regions. Upon oxidative stress, interacts with tumor suppressors TP53 and TP73 in a NADH-dependent way and inhibits their ubiquitin-independent degradation by the 20S proteasome (PubMed:15687255, PubMed:28291250).
Biological Process
AgingIEA:Ensembl
Cell redox homeostasisManual Assertion Based On ExperimentIEP:UniProtKB
Cellular response to hydrogen peroxideIEA:Ensembl
Cellular response to metal ionIEA:Ensembl
Cellular response to oxidative stressManual Assertion Based On ExperimentIDA:UniProtKB
NADH oxidationIEA:Ensembl
NADPH oxidationIEA:Ensembl
Negative regulation of apoptotic processIEA:Ensembl
Negative regulation of catalytic activityIEA:Ensembl
Negative regulation of cellular protein catabolic processManual Assertion Based On ExperimentIDA:UniProtKB
Nitric oxide biosynthetic processManual Assertion Based On ExperimentTAS:ProtInc
Positive regulation of neuron apoptotic processIEA:Ensembl
Removal of superoxide radicalsManual Assertion Based On ExperimentIDA:UniProtKB
Response to alkaloidIEA:Ensembl
Response to amineIEA:Ensembl
Response to carbohydrateIEA:Ensembl
Response to electrical stimulusIEA:Ensembl
Response to estradiolIEA:Ensembl
Response to ethanolIEA:Ensembl
Response to flavonoidIEA:Ensembl
Response to hormoneIEA:Ensembl
Response to hydrogen sulfideIEA:Ensembl
Response to ischemiaIEA:Ensembl
Response to L-glutamineIEA:Ensembl
Response to nutrientIEA:Ensembl
Response to oxidative stressManual Assertion Based On ExperimentIEP:UniProtKB
Response to testosteroneIEA:Ensembl
Response to tetrachloromethaneIEA:Ensembl
Response to toxic substanceManual Assertion Based On ExperimentTAS:ProtInc
Synaptic transmission, cholinergicManual Assertion Based On ExperimentTAS:ProtInc
Ubiquinone metabolic processManual Assertion Based On ExperimentIDA:UniProtKB
Vitamin E metabolic processManual Assertion Based On ExperimentIDA:UniProtKB
Vitamin K metabolic processManual Assertion Based On ExperimentIDA:UniProtKB
Xenobiotic metabolic processManual Assertion Based On ExperimentTAS:ProtInc
Cellular Location
Cytoplasm, cytosol
More Infomation

Preethi, S., Arthiga, K., Patil, A. B., Spandana, A., & Jain, V. (2022). Review on NAD (P) H dehydrogenase quinone 1 (NQO1) pathway. Molecular Biology Reports, 49(9), 8907-8924.

Tsvetkov, P., Adler, J., Strobelt, R., Adamovich, Y., Asher, G., Reuven, N., & Shaul, Y. (2021). NQO1 binds and supports SIRT1 function. Frontiers in pharmacology, 12, 671929.

Rashid, M. H., Babu, D., & Siraki, A. G. (2021). Interactions of the antioxidant enzymes NAD (P) H: Quinone oxidoreductase 1 (NQO1) and NRH: Quinone oxidoreductase 2 (NQO2) with pharmacological agents, endogenous biochemicals and environmental contaminants. Chemico-Biological Interactions, 345, 109574.

Lee, W. S., Ham, W., & Kim, J. (2021). Roles of NAD (P) H: quinone oxidoreductase 1 in diverse diseases. Life, 11(12), 1301.

Ross, D., & Siegel, D. (2021). The diverse functionality of NQO1 and its roles in redox control. Redox Biology, 41, 101950.

Nemeikaitė-Čėnienė, A., Šarlauskas, J., Misevičienė, L., Marozienė, A., Jonušienė, V., Lesanavičius, M., & Čėnas, N. (2020). Aerobic cytotoxicity of aromatic N-oxides: The role of NAD (P) H: quinone oxidoreductase (NQO1). International journal of molecular sciences, 21(22), 8754.

Tsao, Y. C., Chang, Y. J., Wang, C. H., & Chen, L. (2020). Discovery of isoplumbagin as a novel NQO1 substrate and anti-cancer quinone. International journal of molecular sciences, 21(12), 4378.

Glorieux, C., & Calderon, P. B. (2019). Cancer cell sensitivity to redox-cycling quinones is influenced by NAD (P) H: quinone oxidoreductase 1 polymorphism. Antioxidants, 8(9), 369.

Selvakumar, R., Krishnan, D. A., Ramakrishnan, C., Velmurugan, D., & Gunasekaran, K. (2019). Identification of novel NAD (P) H dehydrogenase [quinone] 1 antagonist using computational approaches. Journal of Biomolecular Structure and Dynamics.

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For research use only. Not intended for any clinical use.

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