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Along with the enzymes encoded by the INDO (MIM 147435) and TDO2 (MIM 191070) genes, the enzyme encoded by the INDOL1 gene metabolizes tryptophan in the kynurenine pathway (Ball et al., 2007 [PubMed 17499941]).[supplied by OMIM, Feb 2011].. Additionally we are shipping IDO2 Proteins (8) and IDO2 Kits (4) and many more products for this protein.
Showing 10 out of 120 products:
Human Polyclonal IDO2 Primary Antibody for EIA, IHC (p) - ABIN952817
Cetindere, Nambiar, Santourlidis, Essmann, Hassan: Induction of indoleamine 2, 3-dioxygenase by death receptor activation contributes to apoptosis of melanoma cells via mitochondrial damage-dependent ROS accumulation. in Cellular signalling 2009
Show all 5 references for ABIN952817
Cow (Bovine) Polyclonal IDO2 Primary Antibody for EIA, WB - ABIN401520
Metz, Duhadaway, Kamasani, Laury-Kleintop, Muller, Prendergast: Novel tryptophan catabolic enzyme IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan. in Cancer research 2007
Mouse (Murine) Polyclonal IDO2 Primary Antibody for IHC, ELISA - ABIN1043908
Wolff, Driever, Erdlenbruch, Kortmann, Rutkowski, Pietsch, Parker, Metz, Gnekow, Kramm: Intensive chemotherapy improves survival in pediatric high-grade glioma after gross total resection: results of the HIT-GBM-C protocol. in Cancer 2010
functional importance of IDO (show IDO1 Antibodies) enzymes in human Crohn's disease
Human indoleamine 2,3-dioxygenase-2 has substrate specificity and inhibition characteristics distinct from those of indoleamine 2,3-dioxygenase-1 (show IDO1 Antibodies)
These results demonstrate that IDO2 plays a novel role as a negative regulator of IDO1 (show IDO1 Antibodies) by competing for heme-binding with IDO1 (show IDO1 Antibodies).
The IDO2 is now known to catalyze the first and rate-limiting step in the catabolism of tryptophan along a relative newcomer to the kynurenine pathway field.
Multiple-scattering (MS) analysis of EXAFS data on met-indoleamine 2,3-dioxygenase-2 (IDO2) and analysis of XANES have provided the first direct structural information about the axial donor ligands of the iron center for this recently discovered protein.
IDO2 is expressed in both mDCs and plasmacytoid DCs and is not modulated by PGE2. IDO2 expression is constitutively, stably expressed in steady-state conditions and may contribute to the homeostatic tolerogenic capacity of DCs.
Indoleamine2,3-dioxygenase and tryptophanyl-tRNA synthetase (show WARS Antibodies) may play critical roles in the immune pathogenesis of chronic kidney disease.
Purification and kinetic characterization of human indoleamine 2,3-dioxygenases 1 and 2 (IDO1 (show IDO1 Antibodies) and IDO2) and discovery of selective IDO1 (show IDO1 Antibodies) inhibitors.
Data show that IDO2-specific T cells are cytotoxic effector cells that recognize and kill tumor cells.
Tryptophan supplementation was able to completely restore hepatitis b virus replication in IFN-gamma (show IFNG Antibodies)- but not IFN-alpha (show IFNA Antibodies)-treated cells, which strongly argues that IDO (show IDO1 Antibodies) is the primary mediator of IFN-gamma (show IFNG Antibodies)-elicited antiviral response in human hepatocytes.
Ido2 may be important for mouse embryo implantation and decidualization.
The data showed that there is not significant effect of IDO1 (show IDO1 Antibodies) or TDO2 (show TDO2 Antibodies) on mortality in pneumococcal meningitis.
IDO2 is critical for IDO1 (show IDO1 Antibodies)-mediated T-cell regulation and exerts a non-redundant function in inflammation.
Deletion of Ido1 (show IDO1 Antibodies) and reduced mRNA expression for Ido2 neither affected the concentration of the downstream metabolites of tryptophan nor mRNA expression for downstream genes on the kynurenine pathway in inguinal lymph nodes.
results provide important insights into IDO2 function by defining its pathogenic contributions to autoantibody-mediated autoimmunity.
Immunohistochemical analysis in Ido1 (show IDO1 Antibodies)(-/-) mouse epididymis showed that Ido2 protein was extensively upregulated due to the loss of Ido1 (show IDO1 Antibodies) expression.
IDO-1 (show IDO1 Antibodies) and IDO-2 play biologically important, contradictory roles during intracellular protozoal infection - facilitating (Toxoplasma gondii) or suppressing (Leishmania major) microbial clearance in a pathogen-specific manner.
Findings implicate novel IDO (show IDO1 Antibodies) related enzyme IDO2 in cancer as a result of its preferential inhibition by the D racemer of 1-methyl-tryptophan, used widely in its racemic form (D,L-1MT) as an IDO (show IDO1 Antibodies) inhibitor including as an anticancer agent
A second tryptophan catabolic enzyme inducible by IFNg (show IFNG Antibodies), implicated in transcriptional immune regulation (IFNg (show IFNG Antibodies)-driven negative feedback), may limit the pro-inflammatory and anti-proliferative functions(Review)
This article describes the evolutionary relationships between the INDO (show IDO1 Antibodies) and INDOL1 genes. The INDOL1 protein has a distinct expression pattern compared to INDO (show IDO1 Antibodies) and both have the ability to catabolise tryptophan.
Along with the enzymes encoded by the INDO (MIM 147435) and TDO2 (MIM 191070) genes, the enzyme encoded by the INDOL1 gene metabolizes tryptophan in the kynurenine pathway (Ball et al., 2007
indoleamine 2,3-dioxygenase 2
, indoleamine 2,3-dioxygenase 2-like
, indoleamine 2,3-dioxygenase-like 1 protein
, indoleamine 2,3-dioxygenase-like protein 1
, indoleamine-pyrrole 2,3 dioxygenase-like 1
, indoleamine-pyrrole 2,3-dioxygenase-like protein 1