DHODH Antibody (monoclonal) (M01)
Mouse monoclonal antibody raised against a partial recombinant DHODH.
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC, E |
---|---|
Primary Accession | Q02127 |
Other Accession | NM_001361 |
Reactivity | Human |
Host | mouse |
Clonality | Monoclonal |
Isotype | IgG2a Lambda |
Clone Names | 60 |
Calculated MW | 42867 Da |
Gene ID | 1723 |
---|---|
Other Names | Dihydroorotate dehydrogenase (quinone), mitochondrial, DHOdehase, Dihydroorotate oxidase, DHODH |
Target/Specificity | DHODH (NP_001352, 32 a.a. ~ 140 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa. |
Dilution | WB~~1:500~1000 |
Format | Clear, colorless solution in phosphate buffered saline, pH 7.2 . |
Storage | Store at -20°C or lower. Aliquot to avoid repeated freezing and thawing. |
Precautions | DHODH Antibody (monoclonal) (M01) is for research use only and not for use in diagnostic or therapeutic procedures. |
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Provided below are standard protocols that you may find useful for product applications.
Background
The protein encoded by this gene catalyzes the fourth enzymatic step, the ubiquinone-mediated oxidation of dihydroorotate to orotate, in de novo pyrimidine biosynthesis. This protein is a mitochondrial protein located on the outer surface of the inner mitochondrial membrane.
References
Exome sequencing identifies the cause of a mendelian disorder. Ng SB, et al. Nat Genet, 2010 Jan. PMID 19915526.Dihydroorotate dehydrogenase polymorphism influences the toxicity of leflunomide treatment in patients with rheumatoid arthritis. Grabar PB, et al. Ann Rheum Dis, 2009 Aug. PMID 19605743.The effect of exon (19C>A) dihydroorotate dehydrogenase gene polymorphism on rheumatoid arthritis treatment with leflunomide. Pawlik A, et al. Pharmacogenomics, 2009 Feb. PMID 19207032.Conduct disorder and ADHD: evaluation of conduct problems as a categorical and quantitative trait in the international multicentre ADHD genetics study. Anney RJ, et al. Am J Med Genet B Neuropsychiatr Genet, 2008 Dec 5. PMID 18951430.The structures of human dihydroorotate dehydrogenase with and without inhibitor reveal conformational flexibility in the inhibitor and substrate binding sites. Walse B, et al. Biochemistry, 2008 Aug 26. PMID 18672895.
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