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Human IDO

Also showing Human Tryptophan Catabolic Process to Kynurenine

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated IDO (D5J4E™) Rabbit mAb #86630.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: INDO/IDO1/indoleamine 2,3-dioxygenase (IDO) is an IFN-γ-inducible enzyme that catalyzes the rate-limiting step of tryptophan degradation (1). IDO is upregulated in many tumors and in dendritic cells in tumor-draining lymph nodes. Elevated tryptophan catabolism in these cells leads to tryptophan starvation of T cells, limiting T cell proliferation and activation (2). Therefore, IDO is considered an immunosuppresive molecule, and research studies have shown that upregulation of IDO is a mechanism of cancer immune evasion (3). The gastrointestinal stromal tumor drug, imatinib, was found to act, in part, by reducing IDO expression, resulting in increased CD8+ T cell activation and induction of apoptosis in regulatory T cells (4). In addition to its enzymatic activity, IDO was recently shown to have signaling capability through an immunoreceptor tyrosine-based inhibitory motif (ITIM) that is phosphorylated by Fyn in response to TGF-β. This leads to recruitment of SHP-1 and activation of the noncanonical NF-κB pathway (5).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, IHC-Leica® Bond™, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: INDO/IDO1/indoleamine 2,3-dioxygenase (IDO) is an IFN-γ-inducible enzyme that catalyzes the rate-limiting step of tryptophan degradation (1). IDO is upregulated in many tumors and in dendritic cells in tumor-draining lymph nodes. Elevated tryptophan catabolism in these cells leads to tryptophan starvation of T cells, limiting T cell proliferation and activation (2). Therefore, IDO is considered an immunosuppresive molecule, and research studies have shown that upregulation of IDO is a mechanism of cancer immune evasion (3). The gastrointestinal stromal tumor drug, imatinib, was found to act, in part, by reducing IDO expression, resulting in increased CD8+ T cell activation and induction of apoptosis in regulatory T cells (4). In addition to its enzymatic activity, IDO was recently shown to have signaling capability through an immunoreceptor tyrosine-based inhibitory motif (ITIM) that is phosphorylated by Fyn in response to TGF-β. This leads to recruitment of SHP-1 and activation of the noncanonical NF-κB pathway (5).