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 at4oC.For long-term, aliquot and store at -20oC.Avoid repeated freezing and thawing.