Name :
Recombinant Human IDO Protein
Biological Activity :
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 Immunotherapy Co-inhibitory Immune Checkpoint Targets Immune Checkpoint Immune Checkpoint Detection: ELISA Antibodies Immunotherapy Targeted Therapy
Biological Activity :
Measured by its ability to oxidize L-tryptophan to N-formylk-ynurenine.The specific activity is > 500 pmoles/min/μg.
Expression Host :
Human
Source :
E. coli
Tag :
Protein Accession No. :
NP_002155.1
NCBI Gene ID :
Synonyms :
Synonyms :
indoleamine 2,3-dioxygenase 1
Amino Acid Sequence :
Molecular Weight :
The recombinant human IDO1 consists of 403 amino acids and predicts a molecular mass of 45.2 KDa. It migrates as an approximately 46 KDa band in SDS-PAGE under reducing conditions.
Purity :
> 85 % as determined by SDS-PAGE
State of Matter :
Product Concentration :
Storage and Stability :
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.
Endotoxin Level :
Please contact us for more information.
Protein 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.
Buffer Solution :
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 hardcopy of datasheet.
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.
Redissolution :
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Synonyms :
IDO Protein, Human; IDO-1 Protein, Human; INDO Protein, Human; Indoleamine 2,3‑dioxygenase Protein, Human IDO 背景信息 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 Immunotherapy Co-inhibitory Immune Checkpoint Targets Immune Checkpoint Immune Checkpoint Detection: ELISA Antibodies Immunotherapy Targeted Therapy
References & Citations :
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.
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