Analytical Data
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Gene name
TDO2
- Application
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Alternative Names
TDO2；TDO；Tryptophan 2.3-dioxygenase
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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
P48775
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Expression Region
1-406aa
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AA Sequence
MSGCPFLGNNFGYTFKKLPVEGSEEDKSQTGVNRASKGGLIYGNYLHLEK VLNAQELQSETKGNKIHDEHLFIITHQAYELWFKQILWELDSVREIFQNG HVRDERNMLKVVSRMHRVSVILKLLVQQFSILETMTALDFNDFREYLSPA SGFQSLQFRLLENKIGVLQNMRVPYNRRHYRDNFKGEENELLLKSEQEKT LLELVEAWLERTPGLEPHGFNFWGKLEKNITRGLEEEFIRIQAKEESEEK EEQVAEFQKQKEVLLSLFDEKRHEHLLSKGERRLSYRALQGALMIYFYRE EPRFQVPFQLLTSLMDIDSLMTKWRYNHVCMVHRMLGSKAGTGGSSGYHY LRSTVSDRYKVFVDLFNLSTYLIPRHWIPKMNPTIHKFLYTAEYCDSSYF SSDESD
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Molecular Weight
48 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
TDO2, or tryptophan 2,3-dioxygenase, is an enzyme that plays a crucial role in the catabolism of tryptophan, an essential amino acid. It is primarily found in the liver and is responsible for the oxidative cleavage of tryptophan, which leads to the production of kynurenine and other metabolites involved in various biological processes. Research on TDO2 has gained significant attention due to its implications in several physiological and pathological conditions, including neurodegenerative diseases, cancer, and immunological disorders. Elevated levels of TDO2 have been associated with immune suppression and tumor progression, as the kynurenine pathway can modulate immune responses and promote a tolerogenic environment favorable to tumor growth. Moreover, alterations in tryptophan metabolism are linked to mood disorders and cognitive function, suggesting a potential role for TDO2 in psychiatric conditions. Thus, the study of TDO2 recombinant proteins aims to elucidate the enzyme's structure, function, and biological significance, paving the way for potential therapeutic interventions targeting the kynurenine pathway. Understanding TDO2's mechanisms may lead to novel strategies for treating diseases where tryptophan metabolism is disrupted, offering prospects for improved patient outcomes and novel pharmacological approaches. The ongoing research may also help identify biomarkers for disease prognosis and response to treatment, contributing to personalized medicine in the management of complex health issues.
