Analytical Data
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Gene name
IDO2
- Application
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Alternative Names
IDO2；INDOL1；Indoleamine 2.3-dioxygenase 2
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6ZQW0
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Expression Region
15-420aa
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AA Sequence
EPHRPNVKTAVPLSLESYHISEEYGFLLPDSLKELPDHYRPWMEIA NK LPQLIDAHQLQAHVDKMPLLSCQFLKGHREQRLAHLVLSFLTMGYVWQEG EAQPAEVL PRNLALPFVEVSRNLGLPPILVHSDLVLTNWTKKDPDGFL EIGNLETIISFPGGESLHGF ILVTALVEKEAVPGIKALVQATNAILQP NQEALLQALQRLRLSIQDITKTLGQMHDYVDP DIFYAGIRIFLSGWKD NPAMPAGLMYEGVSQEPLKYSGGSAAQSTVLHAFDEFLGIRHSK ESGD FLYRMRDYMPPSHKAFIEDIHSAPSLRDYILSSGQDHLLTAYNQCVQALA ELRSYH ITMVTKYLITAAAKAKHGKPNHLPGPPQALKDRGTGGTAVMS FLKSVRDKTLESILHPRG
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Molecular Weight
46 kDa
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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
IDO2 (Indoleamine 2,3-dioxygenase 2) is an enzyme that plays a pivotal role in the catabolism of tryptophan, an essential amino acid. It is part of the kynurenine pathway and is primarily expressed in immune cells, such as dendritic cells and macrophages, where it contributes to regulating immune responses and maintaining peripheral tolerance. The research background for IDO2 centers on its potential implications in various diseases, particularly in cancer, autoimmune disorders, and infectious diseases. Unlike the well-studied IDO1, IDO2's functions and mechanisms remain less understood. Preliminary studies suggest that IDO2 may influence T cell functions, thereby modulating the immune microenvironment. Aberrant expression of IDO2 has been associated with tumor progression and immune evasion, making it a potential target for novel immunotherapies. Furthermore, the enzyme's activity may offer insights into neurological conditions due to its connection with neuroactive metabolites derived from tryptophan. Understanding the biochemical pathways and regulatory mechanisms surrounding IDO2 may unveil new therapeutic strategies, emphasizing the need for comprehensive research to elucidate its roles in health and disease.
