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IDO1/Indoleamine 2,3‑dioxygenase  Protein, Antibody, ELISA Kit, cDNA Clone

Description: Active  
Expression host: E. coli  
20 µg 
10 µg 
Add to Cart
  • Slide 1
Expression host: E. coli  
20 µg 
10 µg 
Add to Cart
  • Slide 1

IDO1/Indoleamine 2,3‑dioxygenase Related Area

IDO1/Indoleamine 2,3‑dioxygenase Related Pathways

    IDO1/Indoleamine 2,3‑dioxygenase Summary & Protein Information

    IDO1/Indoleamine 2,3‑dioxygenase Background

    Gene Summary: This gene encodes indoleamine 2,3-dioxygenase (IDO) - a heme enzyme that catalyzes the first and rate-limiting step in tryptophan catabolism to N-formyl-kynurenine. This enzyme acts on multiple tryptophan substrates including D-tryptophan, L-tryptophan, 5-hydroxy-tryptophan, tryptamine, and serotonin. This enzyme is thought to play a role in a variety of pathophysiological processes such as antimicrobial and antitumor defense, neuropathology, immunoregulation, and antioxidant activity. Through its expression in dendritic cells, monocytes, and macrophages this enzyme modulates T-cell behavior by its peri-cellular catabolization of the essential amino acid tryptophan
    General information above from NCBI
    Catalytic activity: D-tryptophan + O(2) = N-formyl-D-kynurenine. {ECO:0000269|PubMed:17671174}.; L-tryptophan + O(2) = N-formyl-L-kynurenine. {ECO:0000269|PubMed:17671174}.
    Cofactor: Name=heme; Xref=ChEBI:CHEBI:30413; ; Note=Binds 1 heme group per subunit.;
    Enzyme regulation: ENZYME REGULATION: Activity is inhibited by and MTH-trp (methylthiohydantoin-DL-tryptophan), modestly inhibited by L-1MT (1-methyl-L-tryptophan) but not D-1MT (1-methyl-D-tryptophan). {ECO:0000269|PubMed:17671174}.
    Induction: By IFNG/IFN-gamma. {ECO:0000269|PubMed:2109605}.
    Sequence similarity: Belongs to the indoleamine 2,3-dioxygenase family. {ECO:0000305}.
    General information above from UniProt

    Indoleamine 2,3-dioxygenase-1, also known as Indoleamine-pyrrole 2,3-dioxygenase, IDO1 and IDO, is a member of the indoleamine 2,3-dioxygenase family. IDO1 / IDO and tryptophan 2,3-dioxygenase (TDO) are tryptophan-degrading enzymes that catalyze the first step in tryptophan catabolism via the kynurenine pathway. TDO is widely distributed in both eukaryotes and bacteria. In contrast, IDO has been found only in mammals and yeast. In 2007, a third enzyme, indoleamine 2,3-dioxygenase-2 (IDO2), was discovered. IDO2 is found not only in mammals but also in lower vertebrates. IDO1 / IDO is an immunosuppressive molecule inducible in various cells. IDO1 / IDO catalyzes the cleavage of the pyrrol ring of tryptophan and incorporates both atoms of a molecule of oxygen. It mediates oxidative cleavage of tryptophan, an amino acid essential for cell proliferation and survival. IDO1 / IDO inhibition is proposed to have therapeutic potential in immunodeficiency-associated abnormalities, including cancer. The IDO pathway is activated in multiple tumor types. Selective inhibition of IDO1 may represent an attractive cancer therapeutic strategy via up-regulation of cellular immunity. IDO1 / IDO is an enzyme that suppresses adaptive T-cell immunity by catabolizing tryptophan from the cellular microenvironment. Inhibition of IDO pathway might enhance the efficacy of immunotherapeutic strategies for cancer.

    Immune Checkpoint
    Immune Checkpoint Detection: ELISA Antibodies
    Co-inhibitory Immune Checkpoint Targets

    Immunotherapy   Cancer Immunotherapy   Targeted Therapy

    IDO1/Indoleamine 2,3‑dioxygenase Alternative Name

    Indoleamine 2,3‑dioxygenase,IDO-1, []
    IDO,IDO1,INDO, [human]
    Ido,Ido1,Indo, [mouse]

    IDO1/Indoleamine 2,3‑dioxygenase Related Studies

  • Barnes NA. et al., 2009, J Immunol. 183 (9): 5768-77.
  • Yuasa HJ. et al., 2009, Comp Biochem Physiol B Biochem Mol Biol. 153 (2): 137-44.
  • L b S. et al., 2009, Cancer Immunol Immunother. 58 (1): 153-7.
  • Liu,X. et al., 2010, Blood.115 (17): 3520-30.
  • Sun,T. et al., 2010, Mol Cell Biochem. 342 (1-2): 29-34.
  • Kiank C. et al., 2010, PLoS One. 5 (7): e11825.