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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. De plus, nous expédions Indoleamine 2,3-Dioxygenase 1 Kits (16) et Indoleamine 2,3-Dioxygenase 1 Protéines (12) et beaucoup plus de produits pour cette protéine.
Showing 10 out of 177 products:
Human Monoclonal IDO1 Primary Antibody pour FACS - ABIN4896116
Kaltenmeier, Gawanbacht, Beyer, Lindner, Trzaska, van der Merwe, Härter, Grüner, Fabricius, Lotfi, Schwarz, Schütz, Hönig, Schulz, Kern, Bommer, Schrezenmeier, Kirchhoff, Jahrsdörfer: CD4+ T cell-derived IL-21 and deprivation of CD40 signaling favor the in vivo development of granzyme B-expressing regulatory B cells in HIV patients. dans Journal of immunology (Baltimore, Md. : 1950) 2015
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Human Polyclonal IDO1 Primary Antibody pour EIA, IHC (p) - ABIN357869
Maghzal, Thomas, Hunt, Stocker: Cytochrome b5, not superoxide anion radical, is a major reductant of indoleamine 2,3-dioxygenase in human cells. dans The Journal of biological chemistry 2008
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Human Polyclonal IDO1 Primary Antibody pour EIA, FACS - ABIN1107630
Grohmann, Fallarino, Puccetti: Tolerance, DCs and tryptophan: much ado about IDO. dans Trends in immunology 2003
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Human Polyclonal IDO1 Primary Antibody pour IHC (p), WB - ABIN389194
Scheler, Wenzel, Tüting, Takikawa, Bieber, von Bubnoff: Indoleamine 2,3-dioxygenase (IDO): the antagonist of type I interferon-driven skin inflammation? dans The American journal of pathology 2007
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Human Monoclonal IDO1 Primary Antibody pour FACS, ICC - ABIN4899442
Bonanno, Mariotti, Procoli, Folgiero, Natale, De Rosa, Majolino, Novarese, Rocci, Gambella, Ciciarello, Scambia, Palumbo, Locatelli, De Cristofaro, Rutella: Indoleamine 2,3-dioxygenase 1 (IDO1) activity correlates with immune system abnormalities in multiple myeloma. dans Journal of translational medicine 2013
Mouse (Murine) Polyclonal IDO1 Primary Antibody pour IHC (fro), IHC (p) - ABIN1107631
Hill, Pereira, Chauveau, Zagani, Remy, Tesson, Mazal, Ubillos, Brion, Asghar, Ashgar, Mashreghi, Kotsch, Moffett, Doebis, Seifert, Boczkowski, Osinaga, Anegon: Heme oxygenase-1 inhibits rat and human breast cancer cell proliferation: mutual cross inhibition with indoleamine 2,3-dioxygenase. dans FASEB journal : official publication of the Federation of American Societies for Experimental Biology 2005
Human Monoclonal IDO1 Primary Antibody pour FACS - ABIN4896118
Lood, Tydén, Gullstrand, Klint, Wenglén, Nielsen, Heegaard, Jönsen, Kahn, Bengtsson: Type I interferon-mediated skewing of the serotonin synthesis is associated with severe disease in systemic lupus erythematosus. dans PLoS ONE 2015
Mouse (Murine) Monoclonal IDO1 Primary Antibody pour FACS, IHC - ABIN1043820
Mellor, Munn: IDO expression by dendritic cells: tolerance and tryptophan catabolism. dans Nature reviews. Immunology 2004
Human Monoclonal IDO1 Primary Antibody pour FACS - ABIN4896114
Chimal-Ramírez, Espinoza-Sánchez, Chávez-Sánchez, Arriaga-Pizano, Fuentes-Pananá: Monocyte Differentiation towards Protumor Activity Does Not Correlate with M1 or M2 Phenotypes. dans Journal of immunology research 2016
Differential expression of CD25 (Montrer IL2RA Anticorps) and IDO mRNA with high and low virulence bovine viral diarrhea virus might reflect temporal differences in transcription during the immune response elicited by these viral strains.
IDO may be involved in downregulating immune responses to M. avium subsp. paratuberculosis and other virulent mycobacteria, which may be an example of the pathogen harnessing host immunoregulatory pathways to aid survival.
INDO participates in IFN-gama-induced death of bovine luteal cells, through a mechanism that involves degradation of tryptophan, thereby reducing tryptophan concentrations to a point insufficient to meet luteal cells needs
SIV-infected macaques exhibiting progression to AIDS displayed greater expression of TGF-beta (Montrer TGFB1 Anticorps) and indoleamine 2,3 dioxygenase in CD8 (Montrer CD8A Anticorps)+ T cells from mesentric lymph nodes.
Our results identified FGL2 (Montrer FGL2 Anticorps), GAL (Montrer GAL Anticorps), SEMA4D (Montrer SEMA4D Anticorps), SEMA7A (Montrer SEMA7A Anticorps), and IDO1 as new candidate genes that could be involved in MSCs-mediated immunomodulation. FGL2 (Montrer FGL2 Anticorps), GAL (Montrer GAL Anticorps), SEMA4D (Montrer SEMA4D Anticorps), SEMA7A (Montrer SEMA7A Anticorps), and IDO1 genes appeared to be differentially transcribed in the different MSC (Montrer MSC Anticorps) populations. Moreover, these genes were not similarly modulated following MSCs-exposure to inflammatory signals
IDO mediated conversion of FOXP3 (Montrer FOXP3 Anticorps) -T cells to Tregs predominantly occurs in children with inflammatory bowel disease.
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.
ver-expression of CTLA4 (Montrer CTLA4 Anticorps) 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.
IDO1 mRNA expression in cervical cancer
IDO gene expression is a feature of aggressive non-muscle-invasive urothelial cell bladder carcinoma, suggesting a potential immunosuppressive role of IDO
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 (Montrer CPT1A Anticorps)).
High IDO1 expression is associated with cervical cancer.
PSG stimulated IDO activity under the conditions of induction of the monocytes by interferon-gamma (Montrer IFNG Anticorps).
These results indicate that the level of IDO expression may be associated with pregnancy-related complications, such as URSA, by affecting trophoblast cell proliferation and migration via the STAT3 (Montrer STAT3 Anticorps) signaling pathway.
Indoleamine-2,3-dioxygenase (IDO) production by Plasmacytoid dendritic cells (pDCs)is necessary to confer suppressive function to T-Cells, Regulatory (Tregs) in experimental autoimmune encephalomyelitis (EAE).
our findings support the hypothesis elevated IDO activity in non-CNS due to virus infections causes pain hypersensitivity
this study shows that IDO overexpression in dendritic cells attenuates acute allograft rejection
This insight into IDO1's involvement in pro-tumorigenic inflammatory neovascularization may have important ramifications for IDO1 inhibitor development, not only in cancer where clinical trials are currently ongoing, but in other disease indications associated with neovascularization as well.
Inhibition of IDO activity ameliorated Japanese encephalitis via enhancement of antiviral IFN-I/II innate and adaptive T-cell responses and increased central nervous system infiltration of peripheral leukocytes.
Results suggest that IDO expression is implicated in immunosuppression and tumor progression in glioma cells; combining IDO inhibition with standard TMZ treatment could be an encouraging therapeutic strategy for patients with malignant glioma
Data show that the expression of indoleamine 2, 3-dioxygenase 1 (IDO) was decreased after tumor cells were infected with Salmonella.
Severity of sodium dodecyl sulfate-induced colitis is reduced in Ido1-deficient mice with down-regulation of TLR-MyD88 (Montrer MYD88 Anticorps)-NF-kB transcriptional networks.
IDO1 deficiency does not affect inflammation in Systemic Juvenile Idiopathic Arthritis, Secondary Hemophagocytic Lymphohistiocytosis and a T cell-triggered cytokine release model.
Data indicate that indolamine-2,3-dioxygenase (IDO) and Fibroblast activation protein alpha (Montrer FAP Anticorps) (FAPalpha) were detectable in B16 melanoma tumor-bearing mice.
This gene encodes indoleamine 2,3-dioxygenase (IDO) - a heme enzyme that catalyzes the first and rate-limiting step in tryptophan catabolism to N-formyl-kynurenine. This enzyme acts on multiple tryptophan substrates including D-tryptophan, L-tryptophan, 5-hydroxy-tryptophan, tryptamine, and serotonin. This enzyme is thought to play a role in a variety of pathophysiological processes such as antimicrobial and antitumor defense, neuropathology, immunoregulation, and antioxidant activity. Through its expression in dendritic cells, monocytes, and macrophages this enzyme modulates T-cell behavior by its peri-cellular catabolization of the essential amino acid tryptophan.
indoleamine-pyrrole 2,3 dioxygenase
, indoleamine 2,3-dioxygenase 2
, putative indoleamine 2,3-dioxygenase
, indoleamine 2,3-dioxygenase 1
, indolamine 2,3 dioxygenase
, indole 2,3-dioxygenase
, indoleamine-pyrrole 2,3-dioxygenase
, indoleamine 23-dioxygenase