Indoleamine 2,3-dioxygenase (IDO) is a heme enzyme that initiates the oxidative degradation of the least abundant, essential amino acid, l-tryptophan, along the kynurenine pathway. This protein is normally expressed in the dendritic cells, macrophages, microglia, eosinophils, fibroblasts, endothelial cells, and most tumor cells. IDO activity is associated with immunosuppression and immune attenuation. Several studies showed that IDO can contribute to immune escape when expressed directly in tumor cells or when expressed in immunosuppressive antigen presenting cells such as tolerogenic dendritic cells or tumor associated macrophages. IDO also is a promising therapeutic target for the treatment of cancer, chronic viral infections, and other diseases characterized by pathological immune suppression.
Measured by its ability to oxidize L-tryptophan to N-formyl-kynurenine. The specific activity is 5166.667 pmol/min/µg pmol/min/µg.
Endotoxin:
<1.0 EU per µg as determined by the LAL method.
Protein Construction:
Recombinant Human Indoleamine 2,3-dioxygenase is produced by our E.coli expression system and the target gene encoding Met1-Gly403 is expressed with a 6His tag at the N-terminus.
Purity:
> 95 % as determined by reducing SDS-PAGE.
Mol Mass:
46.8 kDa
AP Mol Mass:
40-50 kDa
Formulation:
Supplied as a 0.2 µm filtered solution of 20mM Sodium Acetate, 150mM NaCl and 20% Glycerol, pH4.5.
Shipping:
This product is provided as liquid. It is shipped at frozen temperature with blue ice/gel packs.Upon receipt, store it immediately at<-20°C.
Stability and Storage:
Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles.
system_update_altDatasheetMouse IDO1/IDO Recombinant Protein Indoleamine 2,3-dioxygenase (IDO) is a heme enzyme that initiates the oxidative degradation of the least abundant, essential amino aci