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- Tel: 858.663.9055
- Email: info@nsjbio.com
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Indoleamine 2,3-dioxygenase, also called INDO or IDO, is an immunomodulatory enzyme produced by some alternatively activated macrophages and other immunoregulatory cells. This enzyme catalyzes the degradation of the essential amino acid L-tryptophan to N-formyl-kynurenine. By fluorescence in situ hybridization, the assignment is narrowed to chromosome 8p12-p11. IDO-Interferon-gamma interaction has an antiproliferative effect on many tumor cells and inhibits intracellular pathogens such as Toxoplasma and chlamydia, at least partly because of the induction of indoleamine 2,3-dioxygenase. During inflammation, IDO is upregulated in dendritic cells and phagocytes by proinflammatory stimuli, most notably IFNG, and the enzyme then uses superoxide as a 'cofactor' for oxidative cleavage of the indole ring of tryptophan, yielding an intermediate that deformylates to L-kynurenine.
The stated application concentrations are suggested starting amounts. Titration of the IDO antibody may be required due to differences in protocols and secondary/substrate sensitivity.
An amino acid sequence from the N-terminus of human Indoleamine 2, 3-dioxygenase (MAHAMENSWTISKEYHIDEE) was used as the immunogen for this IDO antibody.
After reconstitution, the IDO antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.
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