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 catalyze the first step in tryptophan catabolism via the kynurenine pathway. TDO is present in both eukaryotes and bacteria, whereas IDO has been discovered only in humans and yeast. A third enzyme, indoleamine 2,3-dioxygenase-2 (IDO2), was discovered in 2007. 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, incorporating 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 may have therapeutic use in immunodeficiency-related disorders, such as cancer. The IDO pathway is active in a number of different types of cancer. Through increased cellular immunity, selective blockade of IDO1 may be a desirable cancer treatment approach. IDO1 / IDO is an enzyme that suppresses adaptive T-cell immunity by catabolizing tryptophan from the cellular microenvironment. The immunotherapeutic effects of inhibiting the IDO pathway may be enhanced. IDO1/IDO Recombinant Protein (Gly&Ala2-Gly403) is a highly pure recombinant protein developed by Assay Genie for use in a range of applications.
Product Name:
IDO1/IDO Recombinant Protein (Gly&Ala2-Gly403) (RPES1162)
