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 27, 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 pyrrole 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.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: ELISA AntibodiesImmunotherapyTargeted Therapy
Pack Size | Availability | Price/USD | Quantity |
---|---|---|---|
50 μg | 5 days | $ 498.00 |
Description | 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 27, 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 pyrrole 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.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: ELISA AntibodiesImmunotherapyTargeted Therapy |
Species | Human |
Expression System | E. coli |
Tag | Tag Free |
Accession Number | A0A348GSI3 |
Synonyms | IDO-1, Indoleamine 2,3‑dioxygenase, indoleamine 2,3-dioxygenase 1, IDO, INDO |
Construction | A DNA sequence encoding the human IDO1 (NP_002155.1) (Ala2-Gly403) was expressed and purified with one additional amino acids (Gly) at the N-terminus. |
Protein Purity | > 85 % as determined by SDS-PAGE |
Molecular Weight | 45.2 kDa (predicted) |
Endotoxin | Please contact us for more information. |
Formulation | Supplied as sterile 50 mM NaAC, 100 mM Nacl, 20 % glycerol, pH 5. 5. Please contact us for any concerns or special requirements. Please refer to the specific buffer information in the hard copy of CoA. |
Reconstitution | A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information. |
Stability & Storage |
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |
Shipping |
Kinases are highly recommended to be shipped at frozen temperature with blue ice or dry ice. Shipment made at ambient temperature may seriously affect the activity of the ordered products. |
Research Background | 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 27, 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 pyrrole 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.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: ELISA AntibodiesImmunotherapyTargeted Therapy |
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Please read the User Guide of Recombinant Proteins for more specific information.
IDO Protein, Human, Recombinant IDO-1 Indoleamine 2,3‑dioxygenase indoleamine 2,3-dioxygenase 1 IDO IDO1 INDO IDO 1 recombinant recombinant-proteins proteins protein