Indoleamine 2,3-dioxygenase-1 (Indoleamine-pyrrole 2,3-dioxygenase/IDO1/IDO) is a member of the indoleamine 2,3-dioxygenase family. IDO1 / IDO and tryptophan 2,3-dioxygenase (TDO) are tryptophan-degrading enzymes that act as the first step in the kynurenine pathway. TDO is found in both eukaryotes and bacteria. IDO, on the other hand, has been identified only in humans and yeasts. In 2007, a third enzyme, indoleamine 2,3-dioxygenase-2 (IDO2), was discovered. IDO2 is present in higher vertebrates as well as lower vertebrates. In various cells, IDO is an immunosuppressive molecule that can be induced. The enzyme IDO1, which is also known as IDO, cleaves the pyrrol ring from tryptophan and incorporates both atoms of oxygen in a molecule. 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 active in a variety of tumors. Selective inhibition of IDO1 may be a promising cancer treatment strategy by enhancing cellular immunity. IDO1 / IDO is an enzyme that suppresses adaptive T-cell immunity by catabolizing tryptophan from the cellular microenvironment. The inhibition of the IDO pathway may improve the efficacy of immunotherapeutic approaches for cancer. Human IDO1/IDO Recombinant Protein is a highly pure recombinant protein developed by Assay Genie for use in a range of applications.
