Analytical Data
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Gene name
IDO
- Application
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Alternative Names
CD107B; INDO; Indoleamine-Pyrrole 2,3 Dioxygenase
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P14902
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Expression Region
Ala2~Gly403
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Molecular Weight
43kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
IDO (indoleamine 2,3-dioxygenase) is an enzyme that plays a crucial role in the metabolism of tryptophan, an essential amino acid, by catalyzing its conversion into kynurenine. This metabolic pathway is integral to various physiological processes, particularly in the regulation of immune responses and in the maintenance of immune tolerance. In recent years, research has highlighted the significance of IDO in cancer biology, autoimmune diseases, and transplantation. Tumor cells often exploit IDO to suppress the immune system, thereby evading detection and destruction by immune cells. Furthermore, elevated IDO activity has been associated with chronic inflammation and neurodegenerative disorders. As a result, IDO has garnered attention as a potential therapeutic target, with efforts directed towards developing IDO inhibitors to enhance anti-tumor immunity or modulate immune responses in other pathological conditions. Recombination techniques have been employed to produce IDO as a recombinant protein, facilitating the study of its structure-function relationships, enzyme kinetics, and the development of IDO-based therapeutic interventions. Understanding the molecular mechanisms underlying IDO's activity and its effects on various biological systems could provide insights into new therapeutic strategies for treating a wide array of diseases. Researchers are keen to explore how manipulating IDO pathways can alter disease outcomes, paving the way for innovative treatments that leverage the enzyme's function in immune modulation and metabolic regulation.
