NQO2 Antibody (YA2287)
(Synonyms: QR2; DHQV; DIA6; NMOR2)NQO2 Antibody (YA2287) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to NQO2.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, FC
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
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Conjugation:
Non-conjugated
Applications
| Application |
WB
WB: Western Blot
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FC
FC: Flow Cytometry
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|---|---|---|
| Dilution Ratio | 1:1000-1:2000 | 1:50-1:100 |
Product Details
NQO2 Antibody (YA2287) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to NQO2.
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Host Rabbit
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Clonality Recombinant,Monoclonal
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Species ReactivityHuman, Mouse, Rat
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Observed Molecular WeightObserved band size: 26 kDaNote: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 26 kDa
Entrez Gene: 4835 Human ; 18105 Mouse ; 291084 Rat
SwissProt: P16083 Human ; Q9JI75 Mouse ; Q6AY80 Rat
OMIM: 160998 Human
A synthesized peptide derived from human NQO2 aa1-50.
Endogenous
Affinity Chromatography
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
NQO2 (quinone reductase 2, QR2) is a flavin adenine dinucleotide (FAD) -dependent oxidoreductase that catalyzes two-electron reduction of quinones and related electron acceptors, thereby participating in cellular redox regulation and quinone metabolism[1][2]. Mechanistically, NQO2 belongs to the quinone oxidoreductase family but differs from many classical reductases because it uses reduced nicotinamide derivatives such as N-ribosyldihydronicotinamide (NRH) rather than NADH or NADPH as efficient electron donors[1][3][4]. This distinctive cofactor specificity has driven interest in NQO2 as a regulator of redox biology, reactive oxygen species generation, and cellular metabolic responses[3][4]. In disease-relevant settings, altered NQO2 expression and activity have been associated with oxidative stress-related processes, neurodegeneration, learning and memory regulation, and Alzheimer’s disease-related phenotypes[5][6]. Experimental studies further indicate that genetic or pharmacological suppression of NQO2 can reduce metabolic burden and oxidative stress while improving disease-associated phenotypes in preclinical models[6]. Compared with the closely related isoform NQO1, NQO2 shares structural homology and overlapping substrate classes but exhibits fundamentally different cofactor utilization, making it an atypical oxidoreductase with distinct biological functions and regulatory properties[1][3][4]. For experimental applications, NQO2 has attracted considerable attention as a druggable target, and selective inhibitors including S29434, resveratrol-derived compounds, and other mechanism-based ligands have been developed to probe NQO2-dependent pathways and evaluate therapeutic relevance in redox-associated disorders[7][8].
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Subcellular Localization
Cytoplasm
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Subunit
Homodimer
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SwissProt ID
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Synonyms
QR2; DHQV; DIA6; NMOR2
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Research Field
Signal Transduction
Documentation
References
[1]. Chen S, et al. Structure-function studies of DT-diaphorase (NQO1) and NRH: quinone oxidoreductase (NQO2). Free Radic Biol Med. 2000 Aug;29(3-4):276-84. [Content Brief]
[2]. Lee MJ, et al. Time to HIV rebound after infusion of long-acting broadly neutralising antibodies 3BNC117-LS and 10-1074-LS and analytical treatment interruption (the RIO trial): a double-blind, randomised, placebo-controlled trial. Lancet HIV. 2026 May 27:S2352-3018(26)00059-7. [Content Brief]
[3]. Islam F, et al. The Unusual Cosubstrate Specificity of NQO2: Conservation Throughout the Amniotes and Implications for Cellular Function. Front Pharmacol. 2022 Apr 20;13:838500. [Content Brief]
[4]. Janda E, et al. Polymorphisms and Pharmacogenomics of NQO2: The Past and the Future. Genes (Basel). 2024 Jan 10;15(1):87. [Content Brief]
[5]. Guimera AM, et al. Modelling the role of redox-related mechanisms in musculoskeletal ageing. Free Radic Biol Med. 2019 Feb 20;132:11-18. [Content Brief]
[6]. Gould NL, et al. Specific quinone reductase 2 inhibitors reduce metabolic burden and reverse Alzheimer's disease phenotype in mice. J Clin Invest. 2023 Oct 2;133(19):e162120. [Content Brief]
[7]. Cash JN, et al. Discovery of Small Molecules That Target the Phosphatidylinositol (3,4,5) Trisphosphate (PIP3)-Dependent Rac Exchanger 1 (P-Rex1) PIP3-Binding Site and Inhibit P-Rex1-Dependent Functions in Neutrophils. Mol Pharmacol. 2020 Mar;97(3):226-236. [Content Brief]
[8]. Mattmann ME, et al. Potent and selective synthetic modulators of a quorum sensing repressor in Pseudomonas aeruginosa identified from second-generation libraries of N-acylated L-homoserine lactones. Chembiochem. 2011 Apr 11;12(6):942-9. [Content Brief]