Recombinant Human Tryptophan 2,3-Dioxygenase (TDO2) Protein (His-SUMO)

Name: Recombinant Human Tryptophan 2,3-Dioxygenase (TDO2) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-10804P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Tryptophan 2,3-Dioxygenase (TDO2) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P48775
Target Symbol	TDO2
Synonyms	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)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MSGCPFLGNNFGYTFKKLPVEGSEEDKSQTGVNRASKGGLIYGNYLHLEKVLNAQELQSETKGNKIHDEHLFIITHQAYELWFKQILWELDSVREIFQNGHVRDERNMLKVVSRMHRVSVILKLLVQQFSILETMTALDFNDFREYLSPASGFQSLQFRLLENKIGVLQNMRVPYNRRHYRDNFKGEENELLLKSEQEKTLLELVEAWLERTPGLEPHGFNFWGKLEKNITRGLEEEFIRIQAKEESEEKEEQVAEFQKQKEVLLSLFDEKRHEHLLSKGERRLSYRALQGALMIYFYREEPRFQVPFQLLTSLMDIDSLMTKWRYNHVCMVHRMLGSKAGTGGSSGYHYLRSTVSDRYKVFVDLFNLSTYLIPRHWIPKMNPTIHKFLYTAEYCDSSYFSSDESD
Expression Range	1-406aa
Protein Length	Full Length
Mol. Weight	63.9kDa
Research Area	Metabolism
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.
Protein Families	Tryptophan 2,3-dioxygenase family
Database References	HGNC: 11708 OMIM: 191070 KEGG: hsa:6999 STRING: 9606.ENSP00000444788 UniGene: Hs.183671

Gene Functions References

TDO2 overexpression was related to poor prognosis and associated with cancer cell proliferation and tumor stem cells in esophageal squamous cell carcinoma. PMID: 30134247
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
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
High TDO2 expression is associated with Colorectal Cancer. PMID: 27578919
Crystal tryptophan 2,3-dioxygenase structure revealed eight residues playing critical roles in L-tryptophan oxidation. PMID: 25066423
IL-1beta is suggested to stimulate tryptophan catabolism and production of IL-6 and IL-8 by increasing TDO expression in endometriosis. PMID: 24974860
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
TDO is highly expressed in the brains of Alzheimer disease patients. PMID: 23630570
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
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
Studies indicate that the heme dioxygenases are differentiated by their ability to catalyze the oxidation of l-tryptophan to N-formylkynurenine. PMID: 21361337
subtle differences between the TDO and IDO reactions PMID: 20361220
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
Polymorphism of tryptophan 2,3 dioxygenase gene is associated with autism. PMID: 14755447
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
significant mechanistic differences exist across the heme dioxygenase family, and the data are discussed within this broader framework PMID: 18370401
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
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

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.