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Validated All-in-One™ qPCR Primer for IDO1(NM_002164.5) Search again
Product ID:
HQP055475
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
IDO, IDO-1, INDO
Gene Description:
indoleamine 2,3-dioxygenase 1
Target Gene Accession:
NM_002164.5(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
Gamma-interferon (IFNG; MIM 147570) has an antiproliferative effect on many tumor cells and inhibits intracellular pathogens such as Toxoplasma and Chlamydia, at least partly because of the induction of indoleamine 2,3-dioxygenase (INDO; EC 1.13.11.52). This enzyme catalyzes the degradation of the essential amino acid L-tryptophan to N-formyl-kynurenine.[supplied by OMIM].
Gene References into function
- heme environment--structural properties and substrate-ligand interactions
- Data show that overexpression of indoleamine-2,3-dioxygenase is present in Crohn's disease as well as in ulcerative colitis, but nit in diverticulitis, as compared to normal mucosa.
- inhibition of allogeneic T cell proliferation by indoleamine 2,3-dioxygenase-expressing dendritic cells: mediation of suppression by tryptophan metabolites
- describe a subset of human monocyte-derived dendritic cells that use IDO to inhibit T cell proliferation in vitro
- Induction of IDO in airway epithelial-like tumor cells by exposure to IFN-gamma for 24 hr markedly amplifies IL-6 and IL-8 responses via depletion of tryptophan from the culture medium.
- Asp274 and his346 are essential for heme binding and catalytic function of human indoleamine 2,3-dioxygenase
- Data show that indoleamine 2,3-dioxygenase-expressing fibroblasts embedded within collagen gel suppress the proliferation of allogenic immune cells, while they still remain viable in a tryptophan-deficient culture environment.
- one important consequence of increasing IDO activity in astroglial cells during inflammation is to maintain NAD levels through de novo synthesis from tryptophan.
- characterization of regulatory sequences involved in the synergistic transcriptional activation of the indoleamine dioxygenase gene by interferon-gamma and tumor necrosis factor-alpha.
- Data show that most human tumors constitutively express indoleamine 2,3-dioxygenase (IDO), and that expression of IDO by immunogenic mouse tumor cells prevents their rejection by preimmunized mice.
- indoleamine 2,3-dioxygenase is necessary for cytolytic activity of natural killer cells.
- Downregulation of MHC class I expression by Indoleamine 2,3-dioxygenase(IDO) might be one of the mechanisms through which IDO mediates local immunosuppression.
- Bone marrow stromal cells express IDO protein and exhibit functional IDO activity upon stimulation with IFN-gamma.
- despite suppression by progesterone, indoleamine 2,3-dioxygenase expression in endometrial stromal cells may increase during decidualization due to stimulation by interferon-gamma secreted by infiltrating leukocytes.
- RT4 cells were able to inhibit the growth of Staphylococcus aureus in an IDO-mediated fashion, and this bacteriostatic effect was abolished by endogenously produced NO.
- stimulation with interferon-gamma (IFN-gamma) induces the expression of functionally active IDO in highly purified human epidermal Langerhans cells
- Data suggest that indoleamine 2,3-dioxygenase-mediated suppression by plasmacytoid dendritic cells in tumor-draining lymph nodes creates a local microenvironment that is potently suppressive of host antitumor T cell responses.
- HSV-2 antiviral effect of type II interferon and TNF-alpha is dependent on IDO activation.
- IDO induction in eosinophils is a potential mechanism in the regulation of T helper type 2 (Th2) cell polarization.
- Findings indicate that attenuated Bin1 causes elevation of IDO and immune escape of cancers in mice. Additionally, small molecule inhibitors of IDO reverse the effects of Bin1 loss and leverage the efficacy of chemotherapeutic drugs in cancer.
- IFN-gamma-induced enzyme IDO plays an important antiviral role in Measles Virus infections of epithelial, endothelial, and astroglial cells.
- indoleamine 2,3 dioxygenase (IDO) activity is induced in a two-step process during dendritic cell maturation
- the function of IDO and kynurenine hydroxylase may change from a role in immunosuppression at the maternal-fetal interface in early pregnancy, to one associated with regulation of fetoplacental blood flow or placental metabolism in late gestation
- Indoleamine 2,3-dioxygenase is expressed not by tumor cells, but by normal cells infiltrating the peritumoral stroma
- A high T-helper type 1 (Th1)/Th2 cell ratio is more likely to cause loss of an allogeneic embryo in early pregnancy than is the loss of putative protection by reduced uterine levels of IDO.
- In this review, the unique catalytic properties of indoleamine 2,3-dioxygenase are described, and the recent findings regarding the dioxygenase-initiated tryptophan metabolism are summarized.
- HO-1/IDO cross-regulation modulates apoptosis and proliferation in rat and human breast cancer cells
- examine the arguments for and against a function of IDO-expressing human dendritic cells (DCs) and conclude that proof for an immunoregulatory role in vivo is still lacking
- CTLA-4 on regulatory T cells up-regulates IDO expression on decidual and peripheral blood dendritic cells and monocytes by the induction of IFN-gamma production.
- X-ray crystal structure of human IDO, complexed with the ligand inhibitor 4-phenylimidazole and cyanide was reported.
- IDO significantly contributes to disease progression and overall survival in patients with colorectal cancer.
- purification, crystallization and preliminary X-ray study of human IDO
- Indoleamine 2,3-dioxygenase may have a role in the decline of T cell responses in immunosenescence
- The variable expression of IDO in different endothelial cells is important not only in understanding the role of endothelial cells in the regulation of graft rejection, but also as a potential therapeutic strategy.
- These data provide the first glimpse of the possible regulatory mechanism of hIDO by NO and suggest that the NO-dependent regulation can be modulated by cellular factors, such as the NO abundance, pH, redox environment, and L-Trp availability.
- reduced IDO activity found in the macrophages of patients with hepatitis C virus infection suggest the infection may hamper macrophage functions
- Sleeping beuaty-bsed human indoleamine 2,3-dioxygenase represents a new strategy for treating lung transplantation-associated chronic complications in rats.
- Recombinant antithymocyte globulin inhibits maturation of immature dendritic cells and llows the generation of dendritic cells expressing indoleamine 2,3-dioxygenase.
- Acute myelocytic leukemia cells expresse INDO mRNA, but not IDO protein when exposed to optimal concentrations of IFN-gamma.
- hCG can upregulate human trophoblast indoleamine 2, 3-dioxygenase, which probably plays a key role at maternal fetal interface in preventing fetal rejection.
- IDO activation may protect islet cells from cytotoxic damage by interferon gamma.
- TNF-alpha enhanced TLR ligand-induced IL-8 production in human gingival fibroblasts
- Induction of IDO may dampen T-cell reactivity to viral antigens in chronic hepatitis C virus infection
- change in the clinical course of multiple sclerosis observed in pregnancy may be related to the estrogen-dendritic cell-IDO axis
- CD123/CCR6 dendritic cells (DCs) do not constitutively express IDO and "induced" IDO DCs
- From the expression pattern we conclude that IDO may play a central role in human pregnancies for the establishment of maternal tolerance of fetal antigens
- Review discusses the immunoregulatory pathway of tryptophan catabolism initiated by indoleamine 2,3-dioxygenase (IDO) as a bidirectional feedback loop that could be part of an integrated response for preventing excessive inflammation and autoimmunity.
- IDO expression at the invasive front of cancer cells and APC, and the localization of Foxp3(+) Treg cells in front of cancer tissues, may create a network between IDO and Treg for the
- NO inhibits rhIDO activity reversibly by binding to the active site heme to trap the enzyme as an inactive nitrosyl-Fe(II) enzyme adduct with Trp bound and O2 displaced
- poly(I:C)induction of IDO was mediated in part by IFN-beta but not IFN-gamma, and both NF-kappaB and interferon regulatory factor 3 (IRF3) were required.
- The levels of intralesional expression of mRNA of tumor necrosis factor-alpha, interferon, interleukin-10, RANTES, and indoleamine-2,3-dioxygenase in Mediterranean spotted fever are reported; levels of inducible nitric oxide synthase are also reported.
- Transfected into rats, reduces vascular permeability and leukocyte extravasation, and consequently improves graft function and histologic appearance.
- Interferon gamma-inducible expression of indoleamine 2,3-dioxygenase by human vascular smooth muscle cells inhibits allogeneic T cell activation, proliferation, and accumulation in vitro and in vivo.
- indoleamine 2,3-dioxygenase and prostaglandin E2 represent key mediators of the Mesenchymal stem cells-induced inhibition of NK cells
- The finding of this study revealed that the proliferation of CD8+ and CD4+ T cells are suppressed in response to tryptophan deficient environment caused by IDO expression and it is more so for CD8+ T than CD4+ T cells.
- The present study has demonstrated for the first time that baseline IDO enzymatic activity in induced sputum from asthmatic patients is very low compared with that seen in nonasthmatic control subjects and is inversely related to sputum eosinophilia.
- Any possible antitumor effects of dextro-1-methyl tryptophan cannot be attributed to abrogation of IDO activity in dendritic cells.
- Type I IFN-mediated skin disorders, such as lichen planus , strongly express IDO in lesional skin.
- We submit that an impaired IDO induction characterizes PBC (primary biliary cirrhosis)and might represent a contributing factor in disease pathogenesis in association with several specific defects in the target tissue
- it is suggested that tryptophan depletion via IFN-gamma-mediated IDO induction is a major antibacterial, antiparasitic, antiviral and immunoregulatory mechanism in human lung cells.
- are differences and similarities between biochemical behaviour and structural features of recombinant human IDO and recombinant mouse IDO
- Cytochrome b(5) rather than O(2)(*-) plays a major role in the activation of IDO in human cells.
- transgenic expression of IDO in xenografts contributes to prolonged graft survival
- reveal significant differences between the IDO and tryptophan 2,3-dioxygenase (TDO) enzymes, and the implications of these results are discussed in terms of our current understanding of IDO and TDO catalysis
- IDO may be a novel favorable prognostic indicator and candidate adjuvant therapeutic target for hepatocellular carcinoma.
- IDO is a sensitive marker of atherosclerosis--or the inflammatory response associated with it--but does not have an independent role in the pathogenesis of this disease.
- In patients with acute myeloid leukemia (AML), the serum kynurenine/tryptophan ratio (Kyn/Trp) was raised, suggesting a higher IDO activity than in healthy people
- considerable potential for immunoregulation and antigen-specific tolerance induction in transplantation
- differentiation of naive CD4+ T cells into Tregs with suppressive function was primarily dependent on plasmacytoid dendritic cell expression of indoleamine 2,3-dioxygenase
- IDO pathway is essential for PDC-driven Treg generation from CD4(+)CD25(-) T cells and implicate the generation of kynurenine pathway metabolites as the critical mediator of this process.
- Hydatidiform moles express IDO, but the majority of gestational trophoblastic tumors do not express this enzyme, suggesting that IDO-mediated immunoregulation is unlikely to be a major component of the malignant phenotype in these tumors.
- IDO overexpression in human cancer cells contributes to tumor progression in vivo with suppression of NK cells
- determined INDO mRNA expression in leukemic blasts of 286 patients with acute myeloid leukemia by gene-expression profiling; high INDO expression is a strong negative independent predicting variable for overall and relapse-free survival
- House dust mite-sensitive DCs exposed to Der p 1 downregulated IDO activity and tipped the T(H)1/T(H)2 cytokine balance toward IL-4, resulting in sustainable IDO suppression.
- IDO is critically involved in tumor resistance to repeated treatments with IFNgamma-NGR, likely causing excessive stimulation of tryptophan catabolism and inhibiting antitumor immune mechanisms
- significance of indoleamine 2,3-dioxygenase (IDO) in recurrent breast cancer patients during chemotherapy