Anti-Indoleamine 2, 3-dioxygenase/IDO1 Antibody Picoband® Fluoro488 Conjugated

IDO1 (INDOLEAMINE 2,3-DIOXYGENASE), 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. INDO Interferon-gamma 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.

A synthetic peptide corresponding to a sequence at the N-terminus of human IDO1, different from the related mouse sequence by fourteen amino acids, and from the related rat sequence by seventeen amino acids.

Amino Acid Metabolism, Amino Acids, Atherosclerosis, Cancer, Cardiovascular, Metabolic Signaling Pathways, Metabolism, Pathways and Processes, Signal Transduction, Vascular Inflammation

1. Burkin, D. J., Kimbro, K. S., Barr, B. L., Jones, C., Taylor, M. W., Gupta, S. L. Localization of the human indoleamine 2,3-dioxygenase (IDO) gene to the pericentromeric region of human chromosome 8. Genomics 17: 262-263, 1993. 2. Dai, W., Gupta, S. L. Molecular cloning, sequencing and expression of human interferon-gamma-inducible indoleamine 2,3-dioxygenase cDNA. Biochem. Biophys. Res. Commun. 168: 1-8, 1990. 3. Fallarino, F., Grohmann, U., Hwang, K. W., Orabona, C., Vacca, C., Bianchi, R., Belladonna, M. L., Fioretti, M. C., Alegre, M.-L., Puccetti, P. Modulation of tryptophan catabolism by regulatory T cells. Nature Immun. 4: 1206-1212, 2003.