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Human Polyclonal IDO1 Primary Antibody für ICC, FACS - ABIN1169196
Boasso, Herbeuval, Hardy, Anderson, Dolan, Fuchs, Shearer: HIV inhibits CD4+ T-cell proliferation by inducing indoleamine 2,3-dioxygenase in plasmacytoid dendritic cells. in Blood 2007
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Mouse (Murine) Polyclonal IDO1 Primary Antibody für ICC, IHC - ABIN1169195
Yadav, Burudi, Alirezaei, Flynn, Watry, Lanigan, Fox: IFN-gamma-induced IDO and WRS expression in microglia is differentially regulated by IL-4. in Glia 2007
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Human Monoclonal IDO1 Primary Antibody für 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. in Journal of immunology (Baltimore, Md. : 1950) 2015
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Human Polyclonal IDO1 Primary Antibody für IF (cc), IF (p) - ABIN1714836
Fu, Zhang, Song, Sheng, Li, Li, Song, Wang, Chu, Wei: Effect of bone marrow-derived CD11b(+)F4/80 (+) immature dendritic cells on the balance between pro-inflammatory and anti-inflammatory cytokines in DBA/1 mice with collagen-induced arthritis. in Inflammation research : official journal of the European Histamine Research Society ... [et al.] 2014
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Human Monoclonal IDO1 Primary Antibody für 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. in Journal of immunology research 2016
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Human Monoclonal IDO1 Primary Antibody für 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. in PLoS ONE 2015
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Mouse (Murine) Monoclonal IDO1 Primary Antibody für FACS, IP - ABIN1043733
Mellor, Munn: IDO expression by dendritic cells: tolerance and tryptophan catabolism. in Nature reviews. Immunology 2004
Differential expression of CD25 (zeige IL2RA Antikörper) 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 (zeige TGFB1 Antikörper) and indoleamine 2,3 dioxygenase in CD8 (zeige CD8A Antikörper)+ T cells from mesentric lymph nodes.
PD-L1 (zeige CD274 Antikörper), IDO-1, and B7-H4 (zeige VTCN1 Antikörper) are differentially expressed in human lung carcinomas and show limited co-expression. While PD-L1 (zeige CD274 Antikörper) and IDO-1 are associated with increased tumor-infiltrating lymphoycte and IFN-gamma (zeige IFNG Antikörper) stimulation, B7-H4 (zeige VTCN1 Antikörper) is not.
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).
High IDO1 expression is associated with hepatocellular carcinoma.
Epacadostat significantly decreases Treg proliferation induced by IDO production from IFN-gamma (zeige IFNG Antikörper) plus LPS (zeige IRF6 Antikörper) matured human DCs, although the Treg phenotype does not change
Inhibition of TOR (zeige RORC Antikörper) serine-threonine kinases (mTOR (zeige FRAP1 Antikörper)) strongly induced indoleamine 23-dioxygenase 1 (IDO1) expression and activity, corroborating its ability to recruit Treg cells in the tumor microenvironment.
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.
Despite the large concordance between P and matched M for the evaluated molecular alterations, potential actionable targets such as ESR1 (zeige ESR1 Antikörper) mutations were found only in M. This supports the importance of characterizing the M disease. Other targets we identified, such as HIF1A (zeige HIF1A Antikörper) and IDO1, warrant further investigation in this patient population.
this study demonstrated that the downregulation of IDO expression on the endothelial cells of the villous stroma was associated with preeclampsia
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.
These results show IDO is upregulated with RSV infection and this upregulation likely participates with IFN-gamma (zeige IFNG Antikörper) in inhibition of virus replication and suppression of some host cell responses to infection.
Findings suggest non-redundant neurophysiological roles for indoleamine 2,3-dioxygenase 1, indoleamine 2,3-dioxygenase 2 (zeige IDO2 Antikörper) and tryptophan 2,3-dioxygenase (zeige TDO2 Antikörper) in modulating brain activities and metabolism.
Lipopolysaccharide (LPS (zeige TLR4 Antikörper)) stimulation increased the expression and activity of the immunoregulatory enzyme IDO1 in hepatic stellate cells (HSCs), and LPS (zeige TLR4 Antikörper)/HSCs stimulated aryl hydrocarbon receptor (AhR (zeige AHR Antikörper)) signaling in cocultured regulatory T cells.
this study shows that the presence of IFN-alpha (zeige IFNA Antikörper) at antigen sensitization activates an IDO1/TGF-beta (zeige TGFB1 Antikörper)-dependent anti-inflammatory program that upon antigenic rechallenge prevents inflammation via plasmacytoid dendritic cells
Across strains, networks depicted a predominance of genes under-expressed in microglia relative to macrophages that may be a precursor for the different response of both cell types to challenges. The detected transcriptome differences enhance the understanding of the role of IDO1 in the microglia transcriptome under unchallenged conditions.
Data show that indoleamine 23-dioxygenase 1 (IDO-1) inhibitors 1-methyl-D-tryptophan was able to alleviate most of the behavioural changes resulting from unpredictable chronic mild stress (UCMS) exposure.
IDO did not play a pivotal role in the suppression of allergic airway inflammation through adipose-derived stem cells, suggesting that it is not the major regulator responsible for suppressing allergic airway inflammation.
These results indicate that Platelet-activating Factor -mediated endotoxin tolerance is initiated via IDO- and JAK (zeige JAK3 Antikörper)/STAT (zeige STAT1 Antikörper)-dependent expression of SOCS3 (zeige SOCS3 Antikörper).
Aortic Plasmacytoid dendritic cells expressed CCR9 (zeige CCR9 Antikörper) and indoleamine 2,3-dioxygenase 1 (IDO-1), an enzyme involved in driving the generation of regulatory T cells (Tregs).
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).
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