Recombinant Human IDO1 Protein

Name: Recombinant Human IDO1 Protein
Brand: Beta LifeScience
SKU: BL-1516SG
Availability: InStock

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Tag	GST
Host Species	Human
Accession	BC027882
Synonym	CD107B, IDO, INDO
Background	IDO1 encodes indoleamine 2,3-dioxygenase (IDO) - a heme enzyme that catalyzes the first and rate-limiting step in tryptophan catabolism to N-formyl-kynurenine which acts on multiple tryptophan substrates including D-tryptophan, L-tryptophan, 5-hydroxy-tryptophan, tryptamine, and serotonin. IDO1 play a main role in a variety of pathophysiological processes such as antimicrobial and antitumor defense, neuropathology, immunoregulation, and antioxidant activity. IDO1 activity in tumor cells may act to impair antitumor responses (1). The efficacy of therapeutic vaccination of cancer patients might be improved by concomitant administration of an IDO inhibitor (2).
Description	Full-length recombinant human IDO1 was produced by baculovirus in Sf9 insect cells, fused with a GST tag at N-terminus. This protein is purified with our unique purification methods.
Source	Sf9 insect cells
AA Sequence	Full Length
Molecular Weight	~68 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human IDO1 Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Catalyzes the first and rate limiting step of the catabolism of the essential amino acid tryptophan along the kynurenine pathway. Involved in the peripheral immune tolerance, contributing to maintain homeostasis by preventing autoimmunity or immunopathology that would result from uncontrolled and overreacting immune responses. Tryptophan shortage inhibits T lymphocytes division and accumulation of tryptophan catabolites induces T-cell apoptosis and differentiation of regulatory T-cells. Acts as a suppressor of anti-tumor immunity. Limits the growth of intracellular pathogens by depriving tryptophan. Protects the fetus from maternal immune rejection.
Subcellular Location	Cytoplasm, cytosol.
Protein Families	Indoleamine 2,3-dioxygenase family
Database References	HGNC: 6059 OMIM: 147435 KEGG: hsa:3620 STRING: 9606.ENSP00000430505 UniGene: PMID: 29886172 We discuss how small-molecule inhibitors of the tryptophan (Trp) catabolic enzyme indoleamine 2,3-dioxygenase (IDO) represent a vanguard of new immunometabolic adjuvants to safely enhance the efficacy of cancer immunotherapy, radiotherapy, or 'immunogenic' chemotherapy by leveraging responses to tumor neoantigens PMID: 29413421 The role of IDO1-IDO2-AHR pathway in the TLR4-induced tolerogenic phenotype in human dendritic cells has been reported. PMID: 28256612 High coexpression of cytoplasmic IDO1/COX2 was found to be an independent predictor of poor outcome in colorectal cancer patients. PMID: 29853736 Report the crystal structures of IDO1 in complex with its substrate, Trp, an inhibitor, epacadostat, and/or an effector, indole ethanol (IDE). The data reveal structural features of the active site (Sa) critical for substrate activation; in addition, they disclose a new inhibitor-binding mode and a distinct small molecule binding site (Si). PMID: 29167421 IDO decreased glycolysis and glutaminolysis by activating GCN2K, resulting in activation of AMPactivated protein kinase. PMID: 29693118 this review highlights the role of indoleamine-2,3-dioxygenase in normal and pathological pregnancies PMID: 29154462 Data suggest that IDO1 is constitutively expressed in insulin-secreting cells from donors without diabetes; IDO1 appears to be down-regulated in insulin-containing beta-cells from double autoantibody-positive donors and donors with recent-onset type 1 diabetes; this study was conducted on donor tissues obtained from cadavers. PMID: 29945890 Twenty-nine percent (n = 2/7) of the PD-L1 positive poorly differentiated thyroid carcinomas also co-expressed IDO1 PMID: 29372535 In non-ST segment elevation myocardial infarction, the tolerogenic mechanism of the immune response related to IDO production by activated monocytes derived dendritic cells is altered, supporting their role in T-cell dysregulation. PMID: 29278387 These data suggest that the expression of immunosuppressive molecules, including PD-1 ligands and IDO1, by macrophage/microglia may be involved in immune evasion of lymphoma cells. PMID: 29998979 Our data demonstrate that high intratumoral IDO1 mRNA levels correlate with a poor glioblastoma (GBM) patient prognosis. It also confirms the positive correlation between increased GBM IDO1 levels and human-infiltrating T cells PMID: 28751450 Among the 89 patients, CD274, LAG3, and IDO1 expressions in TIICs were observed in 68.6% (61 cases), 13.5% (12), and 28.1% (25) of patients, respectively. CD274, CTLA4, and IDO1 were expressed in tumor cells of 24.7% (22 cases), 4.5% (4), and 72.0% (64) of patients, respectively. PMID: 29520442 Multivariate analysis indicated indoleamine 2,3-dioxygenase (IDO) expression as independent prognostic factors in overall survival (OS). PMID: 29848687 these findings suggest that IDO1 promoter methylation regulates anti-immune responses in breast cancer subtypes and could be used as a predictive biomarker for IDO1 inhibitor-based immunotherapy. PMID: 28264810 main biological and actionable difference between OSCC from NSND and SD lies in the immune microenvironment, suggesting a higher clinical benefit of PD-L1 and IDO1 inhibition in OSCC from NSND PMID: 28460011 An IDO1 inhibitor, epacadostat also demonstrated promising activity in combination with the PD-1 checkpoint inhibitors in other solid tumors, including melanoma, urothelial carcinoma, renal cell carcinoma, and non-small cell lung cancer PMID: 28760910 This first-in-human phase I study investigated the maximum tolerated dose, safety, pharmacokinetics, pharmacodynamics, and antitumor activity of epacadostat (INCB024360), a potent and selective inhibitor of IDO1 PMID: 28053021 Fumaric acid esters inhibit both IDO expression and enzymatic activity leading to a modulation of tryptophan degradation. PMID: 27376248 Our results highlight the role of COX-2 in constitutive IDO1 expression by human tumors and substantiate the use of COX-2 inhibitors to improve the efficacy of cancer immunotherapy, by reducing constitutive IDO1 expression, which contributes to the lack of T-cell infiltration in "cold" tumors, which fail to respond to immunotherapy PMID: 28765120 this data we have identified the structure of two possible compounds that may be even more potent pharmacological repressors of IDO-1. PMID: 28735627 Prognostic value of IDO in acute myeloid leukemia. PMID: 26762931 These findings indicate that IDO1 has the potential to participate in or contribute to the formation of new capillaries, supporting the applicability of IDO1-targeting molecular therapy in lung cancer. PMID: 28498425 induces PD-L1 expression by melanoma cells PMID: 27121174 PD-L1, IDO-1, and B7-H4 are differentially expressed in human lung carcinomas and show limited co-expression. While PD-L1 and IDO-1 are associated with increased tumor-infiltrating lymphoycte and IFN-gamma stimulation, B7-H4 is not. PMID: 27440266 Data show that indole 23-dioxygenase (IDO) is variably expressed by tumor-infiltrating immune cells or reactive cells rather than lymphoma cells in diffuse large-cell lymphoma (DLBCL). PMID: 26727587 High IDO1 expression is associated with hepatocellular carcinoma. PMID: 26895379 Epacadostat significantly decreases Treg proliferation induced by IDO production from IFN-gamma plus LPS matured human DCs, although the Treg phenotype does not change PMID: 27192116 Inhibition of TOR serine-threonine kinases (mTOR) strongly induced indoleamine 23-dioxygenase 1 (IDO1) expression and activity, corroborating its ability to recruit Treg cells in the tumor microenvironment. PMID: 27174915 up-regulation induces immunosuppression and may enhance the risk of hepatitis C virus and hepatitis B virus induced hepatocellular carcinoma [review] PMID: 28428708 MALAT1-overexpressed MSCs promoted M2 macrophage polarization and this effect was mediated by MALAT1-induced IDO expression, suggesting that MALAT1 may enhance the immunosuppressive properties of MSCs in vivo. PMID: 28176360 this study demonstrated that the downregulation of IDO expression on the endothelial cells of the villous stroma was associated with preeclampsia PMID: 28131097 The data suggest that in Puumala infection, the mechanism responsible for the suppressive effect of IDO is not metabolic control of effector cells but rather the signaling mediated by tryptophan breakdown products, such as kynurenine. PMID: 28057727 These results show IDO is upregulated with RSV infection and this upregulation likely participates with IFN-gamma in inhibition of virus replication and suppression of some host cell responses to infection. PMID: 28963880 IDO role in cancer immune responses [review] PMID: 26517538 This study demonstrated that IDO-1 was elevated in the Solid Component and Cyst Fluid of Human Adamantinomatous Craniopharyngioma. PMID: 28859336 The Binding Mode of N-Hydroxyamidines to Indoleamine 2,3-Dioxygenase 1 PMID: 28731684 Fourier transform infrared (FTIR) and nanosecond time-resolved optical spectroscopy to hIDO1 variants with modified heme pocket structures to identify important amino acid residues that stabilize the substrate in the active site. PMID: 28189796 Thus, our study provides novel insights into the interaction between a small molecule inhibitor INCB14943 and IDO1 protein. The structural information will facilitate future IDO1 inhibitor design. PMID: 28412361 The aim of the present study was to clarify the effect of IDO1induced macrophages on the growth of endometrial stromal cells in endometriosis. IDO1 educated-macrophages may facilitate the survival of retrograde endometrial tissues, and be involved in the pathogenesis of endometriosis. PMID: 28260094 Our results identified FGL2, GAL, SEMA4D, SEMA7A, and IDO1 as new candidate genes that could be involved in MSCs-mediated immunomodulation. FGL2, GAL, SEMA4D, SEMA7A, and IDO1 genes appeared to be differentially transcribed in the different MSC populations. Moreover, these genes were not similarly modulated following MSCs-exposure to inflammatory signals PMID: 28336906 IDO mediated conversion of FOXP3 -T cells to Tregs predominantly occurs in children with inflammatory bowel disease. PMID: 28337881 The study confirmed that high IDO expression in pancreatic adenocarcinoma was related to poor prognosis of patients. These findings provided evidence that IDO was involved in pancreatic adenocarcinoma progression and might serve as a relevant therapeutic target. PMID: 28303855 ver-expression of CTLA4 and IDO1 was significantly associated with biochemical recurrence. Our results provide clues on the mechanisms of tumor development and point to potential biomarkers for early detection and treatment for prostate cancer in young men. PMID: 28027300 IDO1 mRNA expression in cervical cancer PMID: 27761872 Structural Study of a Flexible Active Site Loop in Human Indoleamine 2,3-Dioxygenase and Its Functional Implications. PMID: 27112409 IDO gene expression is a feature of aggressive non-muscle-invasive urothelial cell bladder carcinoma, suggesting a potential immunosuppressive role of IDO PMID: 28314306 Data show that in the absence of indoleamine 2,3-dioxygenase (IDO) inhibition, fatty acid oxidation increased along with increased activity of carnitine palmitoyltransferase I (CPT1). PMID: 27667153 High IDO1 expression is associated with cervical cancer. PMID: 27106797 PSG stimulated IDO activity under the conditions of induction of the monocytes by interferon-gamma. PMID: 27595833

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

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Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

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