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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 Antibodies (123) and IDO2 Proteins (8) and many more products for this protein.
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This study demonstrated that IDO2 rs10109853 and rs4503083 polymorphisms are not associated with MS risk, age at onset and disease progression in Italian MS patients.
High IDO2 expression is associated with Colorectal Cancer.
High IDO2 expression is associated with cervical cancer.
functional importance of IDO (show IDO1 ELISA Kits) 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 ELISA Kits)
These results demonstrate that IDO2 plays a novel role as a negative regulator of IDO1 (show IDO1 ELISA Kits) by competing for heme-binding with IDO1 (show IDO1 ELISA Kits).
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 ELISA Kits) may play critical roles in the immune pathogenesis of chronic kidney disease.
Gene silencing of indoleamine 2,3-dioxygenase 2 in melanoma cells induces apoptosis through the suppression of NAD+ and inhibits in vivo tumor growth.
Findings suggest non-redundant neurophysiological roles for indoleamine 2,3-dioxygenase 1 (show IDO1 ELISA Kits), indoleamine 2,3-dioxygenase 2 and tryptophan 2,3-dioxygenase (show TDO2 ELISA Kits) in modulating brain activities and metabolism.
The IDO2-deficient B cells lacked the ability to upregulate the costimulatory marker CD40 (show CD40 ELISA Kits), suggesting IDO2 acts at the T-B cell interface to modulate the potency of T cell help needed to promote autoantibody production.
Targeting IDO2 with a monoclonal antibody inhibits autoreactive B and T cell activation and alleviates joint inflammation in two well-characterized preclinical models of arthritis.
Indoleamine-2,3-dioxygenase (IDO (show IDO1 ELISA Kits)) production by Plasmacytoid dendritic cells (pDCs)is necessary to confer suppressive function to T-Cells, Regulatory (Tregs) in experimental autoimmune encephalomyelitis (EAE).
Ido2 may be important for mouse embryo implantation and decidualization.
The data showed that there is not significant effect of IDO1 (show IDO1 ELISA Kits) or TDO2 (show TDO2 ELISA Kits) on mortality in pneumococcal meningitis.
IDO2 is critical for IDO1 (show IDO1 ELISA Kits)-mediated T-cell regulation and exerts a non-redundant function in inflammation.
Deletion of Ido1 (show IDO1 ELISA Kits) 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.
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