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

Name: Recombinant Mouse Tryptophan 2,3-Dioxygenase (TDO2) Protein (His)
Brand: Beta LifeScience
SKU: BLC-11218P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Tryptophan 2,3-Dioxygenase (TDO2) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P48776
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	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MSGCPFAGNSVGYTLKNVSMEDNEEDRAQTGVNRASKGGLIYGNYLQLEKILNAQELQSEVKGNKIHDEHLFIITHQAYELWFKQILWELDSVREIFQNGHVRDERNMLKVIARMHRVVVIFKLLVQQFSVLETMTALDFNDFREYLSPASGFQSLQFRLLENKIGVLQSLRVPYNRKHYRDNFGGDYNELLLKSEQEQTLLQLVEAWLERTPGLEPNGFNFWGKFEKNILKGLEEEFLRIQAKTDSEEKEEQMAEFRKQKEVLLCLFDEKRHDYLLSKGERRLSYRALQGALMIYFYREEPRFQVPFQLLTSLMDIDTLMTKWRYNHVCMVHRMLGTKAGTGGSSGYHYLRSTVSDRYKVFVDLFNLSTYLVPRHWVPKMNPIIHKFLYTAEYSDSSYFSSDESD
Expression Range	1-406aa
Protein Length	Full Length
Mol. Weight	53.3 kDa
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.
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: mmu:56720 STRING: 10090.ENSMUSP00000029645 UniGene: Mm.258622

Gene Functions References

TDO-deficiency protected from neuronal loss in the spinal cord but not in the optic nerves. PMID: 28117398
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
Data suggest that Indoleamine 2,3-dioxygenase 1 (IDO1) appears to be a potential hallmark of liver lesions, and its deficiency protects mice from CCl4-induced fibrosis mediated by Th17 cells down-regulation and tryptophan 2,3-dioxygenase (TDO) compensatory increase. PMID: 28465467
Findings suggest non-redundant neurophysiological roles for indoleamine 2,3-dioxygenase 1, indoleamine 2,3-dioxygenase 2 and tryptophan 2,3-dioxygenase in modulating brain activities and metabolism. PMID: 27316339
Data suggest that high-fat diet (HFD) alters regulation of expression of sirtuins (Sirt4 and Sirt7) and enzymes in NAD biosynthetic pathway (Tdo2 and Nnmt); these alterations are more prominent in liver as compared to white adipose tissue or skeletal muscle; Tdo2 and Nnmt may serve as markers of HFD consumption. (Tdo2 = tryptophan 2,3-dioxygenase; Nnmt = nicotinamide N-methyltransferase) PMID: 27592202
both TDO and IDO biosynthesize nicotinamide from D-tryptophan and L-tryptophan in mice PMID: 25035993
Data indicate that tryptophan 2,3-dioxygenase (Tdo2) may play an important role during mouse decidualization and be regulated by estrogen, progesterone, and cAMP. PMID: 24190896
These findings demonstrate a direct molecular link between Trp metabolism and neurogenesis and anxiety-related behavior under physiological conditions. PMID: 19323847
Endometrial expression of TDO in epithelial and stromal cells is regulated by HOXA10. Expression level of TDO influences infiltration of T-cells into endometrial stroma and thus may influence embryo viability. PMID: 20959529
These findings indicate that TDO might be required at a late-stage of granule cell development, such as during axonal and dendritic growth, synaptogenesis and its maturation. PMID: 20815922
No relationship was found between alcohol consumption, Tdo2 activity, and single nucleotide substitution in intron 6 of the Tdo2 gene assoiated with predisposition to alcoholism in humans. PMID: 14714090
Our findings indicate that TDO and its novel variants may play an important role in not only the liver but also in local areas in developing and adult brain. PMID: 19428689

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.