Human Recombinant NQO1 protein, His Tag (V2LY-0526-LY5832)

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Basic Information

Expressed Host
E. coli
Protein Species
Human
Tag
His Tag
Protein Construction
This product is Human Recombinant NQO1 protein, His Tag consist of Amino Acid: 1-274 and predicts a molecular mass of 33 kDa.
Molecule Mass
33 kDa
Verified
HPLC
Sequence
Amino Acid: 1-274
Species
Human

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

Purity
≥90% as determined by SDS-PAGE. ≥95% as determined by SEC-HPLC.
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile PBS
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
NAD(P)H Quinone Dehydrogenase 1
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

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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