NQO2 Antibody (Center)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, E |
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Primary Accession | P16083 |
Reactivity | Human, Mouse |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 25919 Da |
Antigen Region | 141-168 aa |
Gene ID | 4835 |
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Other Names | Ribosyldihydronicotinamide dehydrogenase [quinone], NRH dehydrogenase [quinone] 2, NRH:quinone oxidoreductase 2, Quinone reductase 2, QR2, NQO2, NMOR2 |
Target/Specificity | This NQO2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 141-168 amino acids from the Central region of human NQO2. |
Dilution | WB~~1:1000 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | NQO2 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | NQO2 |
---|---|
Synonyms | NMOR2 |
Function | The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. |
Cellular Location | Cytoplasm. |
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Provided below are standard protocols that you may find useful for product applications.
Background
NQO2 apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis.
References
Foster,C.E., et.al., Biochemistry 38 (31), 9881-9886 (1999)
Wu,K., Knox,R., et.al., Arch. Biochem. Biophys. 347 (2), 221-228 (1997)
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