Analytical Data
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Gene name
TDO
- Application
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Alternative Names
TDO2; TPH2; TO; TRPO; Tryptophanase; Tryptophan oxygenase
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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
P48775
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Expression Region
Met1~Asp406
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Molecular Weight
50kDa
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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
Related Products
Protein Description
TDO (Tryptophan 2,3-dioxygenase) is a key enzyme involved in the kynurenine pathway, which is crucial for tryptophan catabolism. The study of TDO recombinant protein has gained significant interest due to its role in regulating levels of tryptophan and its metabolites, important in various physiological and pathological processes. TDO is primarily expressed in the liver and is responsible for the oxidative cleavage of tryptophan into N-formylkynurenine, which further converts into kynurenine, linking it to immune response modulation, neurodegenerative diseases, and cancer. Abnormal TDO activity has been associated with increased kynurenine levels, leading to immunosuppression and potential tumor progression. Therefore, understanding TDO structure and function through recombinant protein production offers insights into its mechanistic roles in disease. Recent advances in molecular biology techniques have enabled the efficient production of TDO recombinant proteins, allowing for detailed characterization and the development of inhibitors that could mitigate its activity. This research may pave the way for therapeutic strategies targeting TDO to balance tryptophan metabolism in disorders linked to immune dysfunction and neurodegeneration. Overall, the exploration of TDO recombinant protein serves as a promising avenue for both fundamental research and clinical applications.
