Anti-IDO Indoleamine 2, 3-dioxygenase

0.5mg/ml if reconstituted with 0.2ml sterile DI water. 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. Protein function: Catalyzes the first and rate limiting step of the catabolism of the essential amino acid tryptophan along the kynurenine pathway (PubMed:17671174). Involved in the peripheral immune tolerance, contributing to maintain homeostasis by preventing autoimmunity or immunopathology that would result from uncontrolled and overreacting immune responses (PubMed:25691885). Tryptophan shortage inhibits T lymphocytes division and accumulation of tryptophan catabolites induces T-cell apoptosis and differentiation of regulatory T-cells (PubMed:25691885). Acts as a suppressor of anti-tumor immunity (PubMed:23103127, PubMed:25157255, PubMed:14502282, PubMed:25691885). Limits the growth of intracellular pathogens by depriving tryptophan (PubMed:25691885). Protects the fetus from maternal immune rejection (PubMed:25691885). [The UniProt Consortium]