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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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DHODH Polyclonal Antibody recognizes dihydroorotate dehydrogenase (DHODH), a mitochondrial enzyme involved in de novo pyrimidine nucleotide biosynthesis. DHODH catalyzes the oxidation of dihydroorotate to orotate, the fourth enzymatic step in the pathway leading to uridine monophosphate (UMP) production. Pyrimidine nucleotides are essential components of DNA and RNA and contribute to numerous cellular metabolic processes. This Dihydroorotate Dehydrogenase Rabbit Antibody targets a protein that connects nucleotide synthesis with mitochondrial function.
The human DHODH gene is located on chromosome 16 and encodes a protein of approximately 43 kDa. DHODH is associated with the outer surface of the mitochondrial inner membrane, where its catalytic activity depends on flavin mononucleotide (FMN) and ubiquinone. During dihydroorotate oxidation, electrons are transferred to ubiquinone, linking pyrimidine biosynthesis to mitochondrial electron transport. Consequently, changes in respiratory chain activity can influence DHODH function and nucleotide availability.
De novo pyrimidine synthesis is particularly important in rapidly proliferating cells, which require substantial nucleotide supplies for DNA replication and RNA transcription. Although cells can obtain pyrimidines through salvage pathways, their dependence on de novo synthesis varies with metabolic conditions and proliferative activity. DHODH therefore represents an important connection between mitochondrial metabolism, cellular growth, and nucleotide homeostasis.
DHODH is an established therapeutic target in autoimmune and inflammatory disorders. Inhibition of its enzymatic activity reduces pyrimidine nucleotide production and can limit the proliferation of activated lymphocytes. Leflunomide and teriflunomide are examples of clinically used DHODH inhibitors. The enzyme is also being investigated as a potential therapeutic target in cancer because certain malignant cells depend heavily on de novo pyrimidine synthesis. The Dihydroorotate Dehydrogenase Rabbit Antibody is relevant to studies examining these metabolic pathways.
Research involving DHODH contributes to understanding mitochondrial function, nucleotide metabolism, immune cell activation, and cellular proliferation. NSJ Bioreagents offers antibodies targeting metabolic enzymes involved in these biological processes. A DHODH Polyclonal Antibody provides a research tool for examining dihydroorotate dehydrogenase expression and investigating the relationship between pyrimidine biosynthesis and mitochondrial metabolism.
For an alternative monoclonal antibody targeting the same enzyme, see our DHODH Antibody 2G7.
Differences in protocols and secondary/substrate sensitivity may require the DHODH Polyclonal Antibody / Dihydroorotate Dehydrogenase Rabbit Antibody to be titrated for optimal performance.
Amino acids 132-173 (RVFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQKQAKLTED) from the human protein were used as the immunogen for the DHODH Polyclonal Antibody.
After reconstitution, the DHODH Polyclonal Antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.
Dihydroorotate Dehydrogenase antibody, Dihydroorotate Dehydrogenase Polyclonal antibody, Dihydroorotate Oxidase antibody, DHO Dehydrogenase antibody, Mitochondrial Dihydroorotate Dehydrogenase antibody
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