Recombinant Human Tryptophan 2,3-dioxygenase (TDO2)

Code CSB-YP023351HU
Size $250
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Purity
Greater than 90% as determined by SDS-PAGE.
Target Names
TDO2
Uniprot No.
Research Area
Metabolism
Alternative Names
3-dioxygenase; T23O_HUMAN; TDO 2; TDO; tdo2; TO; TPH2; TRPO; Tryptamin 2 3 dioxygenase; Tryptamin 2; Tryptophan 2 3 dioxygenase; Tryptophan 2; Tryptophan oxygenase; Tryptophan pyrrolase; Tryptophanase
Species
Homo sapiens (Human)
Source
Yeast
Expression Region
1-406aa
Target Protein Sequence
MSGCPFLGNNFGYTFKKLPVEGSEEDKSQTGVNRASKGGLIYGNYLHLEKVLNAQELQSETKGNKIHDEHLFIITHQAYELWFKQILWELDSVREIFQNGHVRDERNMLKVVSRMHRVSVILKLLVQQFSILETMTALDFNDFREYLSPASGFQSLQFRLLENKIGVLQNMRVPYNRRHYRDNFKGEENELLLKSEQEKTLLELVEAWLERTPGLEPHGFNFWGKLEKNITRGLEEEFIRIQAKEESEEKEEQVAEFQKQKEVLLSLFDEKRHEHLLSKGERRLSYRALQGALMIYFYREEPRFQVPFQLLTSLMDIDSLMTKWRYNHVCMVHRMLGSKAGTGGSSGYHYLRSTVSDRYKVFVDLFNLSTYLIPRHWIPKMNPTIHKFLYTAEYCDSSYFSSDESD
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
49.9kDa
Protein Length
Full Length
Tag Info
N-terminal 6xHis-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.
Description

In the production of recombinant Human TDO2 protein, the gene for TDO2 (Yeast) was cloned into a vector and expressed as TDO2 protein in Yeast. The plasmids with the copy of TDO2, or the expression vector, were often used to enhance gene expression. Every step of production was undergone with a strict QC system. N-terminal 6xHis tag was used in the process. The purity is 90% determined by SDS-PAGE.

TDO2, indoleamine 2,3-dioxygenase 1 (IDO1), and IDO2 are three enzymes that catalyze the amino acid tryptophan into kynurenine in the kynurenine pathway, which accounts for 95% of tryptophan catabolism. TDO2 is mainly expressed in the liver and exists in the brain, while IDO1 and IDO2 have wider tissue expression, including in peripheral blood and immune cells. TDO2 plays an important role in neurological diseases such as Alzheimer’s disease, Parkinson’s disease, and autism. TDO2 is expressed in several established human cancer cell lines, including glioblastoma, colorectal carcinoma, head and neck carcinoma, and gallbladder carcinoma cells. Overexpression of TDO2 promoted tumor cell survival and was correlated with tumor grade and poor prognosis in triple negative breast cancer and in brain tumors. Besides, expression of TDO2 has been reported in human colorectal cancer and leiomyosarcoma.

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Target Background

Function
Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety.
Gene References into Functions
  1. TDO2 overexpression was related to poor prognosis and associated with cancer cell proliferation and tumor stem cells in esophageal squamous cell carcinoma. PMID: 30134247
  2. Study demonstrated that n-butylidenephthalide (n-BP)functions by regulating the early part of the kynurenine pathway through the downregulation of tryptophan 2, 3-dioxygenase (TDO2), which decreases the downstream neurotoxic product, quinolinic acid (QA). Findings indicate a correlation between n-BP, TDO2, QA, calpain, and toxic fragment formation. PMID: 28223212
  3. the potent antimicrobial as well as immunoregulatory effects of TDO were substantially impaired under hypoxic conditions that pathophysiologically occur in vivo. This might be detrimental for the appropriate host immune response towards relevant pathogens. PMID: 27563172
  4. High TDO2 expression is associated with Colorectal Cancer. PMID: 27578919
  5. Crystal tryptophan 2,3-dioxygenase structure revealed eight residues playing critical roles in L-tryptophan oxidation. PMID: 25066423
  6. IL-1beta is suggested to stimulate tryptophan catabolism and production of IL-6 and IL-8 by increasing TDO expression in endometriosis. PMID: 24974860
  7. Identification of 12 polymorphisms in the human TDO2 promoter region, 2 of them corresponding to previously unknown single-nucleotide polymorphisms and 3 of them located in putative glucocorticoid-responsive elements. PMID: 23558111
  8. TDO is highly expressed in the brains of Alzheimer disease patients. PMID: 23630570
  9. Data suggest that T342 in hTDO has critical role in controlling substrate binding, substrate stereoselectivity, H-bonding interaction between enzyme and intermediates, and regulating the dynamics of protein structure. PMID: 22082147
  10. The data suggest that TDO uses a ring-opening mechanism during N-formylkynurenine formation, rather than Criegee or dioxetane mechanisms as previously proposed. PMID: 21892828
  11. Studies indicate that the heme dioxygenases are differentiated by their ability to catalyze the oxidation of l-tryptophan to N-formylkynurenine. PMID: 21361337
  12. subtle differences between the TDO and IDO reactions PMID: 20361220
  13. The activity and mRNA expression level of indoleamine 2,3-dioxygenase in term placentas were significantly lower in preeclampsia. Could cause dysregulation of inflammatory response intrinsic to normal pregnancy. PMID: 12634647
  14. Polymorphism of tryptophan 2,3 dioxygenase gene is associated with autism. PMID: 14755447
  15. We found that astrocytes, neurons, and microglia expressed IDO but only microglia were able to produce detectable amounts of quinolinic acid. However, astrocytes and neurons had the ability to catabolize quinolinic acid. PMID: 15390107
  16. significant mechanistic differences exist across the heme dioxygenase family, and the data are discussed within this broader framework PMID: 18370401
  17. The tyrosine 42 of recombinant human TDO is responsible for the cooperative binding of l-Trp by participating in the active site of the adjacent subunit. PMID: 19218188
  18. TDO mediates antimicrobial and immunoregulatory effects. TDO-dependent inhibition of T-cell growth might be involved in the immunotolerance observed in vivo during allogeneic liver transplantation. PMID: 19637229

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Protein Families
Tryptophan 2,3-dioxygenase family
Database Links

HGNC: 11708

OMIM: 191070

KEGG: hsa:6999

STRING: 9606.ENSP00000444788

UniGene: Hs.183671

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