Recombinant Rattryptophan 2,3-Dioxygenaseunirule Annotation (TDO2) Protein (His-SUMO)

Name: Recombinant Rattryptophan 2,3-Dioxygenaseunirule Annotation (TDO2) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09379P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Rattryptophan 2,3-Dioxygenaseunirule Annotation (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	P21643
Target Symbol	TDO2
Synonyms	Tdo2; Tdo; Tryptophan 2,3-dioxygenase; TDO; EC 1.13.11.11; Tryptamin 2,3-dioxygenase; Tryptophan oxygenase; TO; TRPO; Tryptophan pyrrolase; Tryptophanase
Species	Rattus norvegicus (Rat)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MSGCPFSGNSVGYTLKNLSMEDNEEDGAQTGVNRASKGGLIYGDYLQLEKILNAQELQSEIKGNKIHDEHLFIITHQAYELWFKQILWELDSVREIFQNGHVRDERNMLKVMTRMHRVVVIFKLLVQQFSVLETMTALDFNDFREYLSPASGFQSLQFRLLENKIGVLQSLRVPYNRKHYRDNFEGDYNELLLKSEQEQTLLQLVEAWLERTPGLEPHGFNFWGKFEKNILKGLEEEFLKIQAKKDSEEKEEQMAEFRKQKEVLLCLFDEKRHDYLLSKGERRLSYRALQGALMIYFYREEPRFQVPFQLLTSLMDIDTLMTKWRYNHVCMVHRMLGSKAGTGGSSGYYYLRSTVSDRYKVFVDLFNLSSYLVPRHWIPKMNPIIHKFLYTAEYSDSSYFSSDESD
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	KEGG: rno:64206 STRING: 10116.ENSRNOP00000015732 UniGene: Rn.1029
Tissue Specificity	Liver.

Gene Functions References

Results show that stress-induced corticosterone and consequent activation of hepatic TDO, tryptophan metabolism and production of kynurenine provoke a depression-related behavioural phenotype PMID: 24472498
tryptophan oxygenase gene might rely on the binding of the enhancer (the -8.5kb S/MAR-GRE) and the promoter to the inner nuclear matrix. PMID: 19632204
Data support the involvement of insulin in modulation of glucocorticoid receptor signaling pathway which mediates, in part, the activity of tryptophan oxygenase. PMID: 17223727
these data show that the nucleosome array in the regulatory region of the actively transcribed tdo gene in vivo is disturbed. PMID: 20737904
The cerebrocortical TDO2 genes were increased in aged rats. Certain age dependent transcriptional changes might influence the mechanism of Alzheimer dis and other neurodegenerative disorders. PMID: 19835274

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.