Product Specifications for Recombinant Mouse TDO2 His-tag Protein, CF
E. coli-derived mouse TDO2 protein Val18-Phe388 with a C terminal 6-His tag
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<0.10 EU per 1 μg of the protein by the LAL method.
N-terminal sequence Analysis
Predicted Molecular Mass
39 & 75 kDa, reducing conditions
Measured by its ability to oxidize L-tryptophan to N-formyl-kynurenine. The specific activity is >500 pmol/min/μg, as measured under the described conditions.
Scientific Data Examples for Recombinant Mouse TDO2 His-tag Protein, CF
Recombinant Mouse TDO2 His-tag Protein Enzyme Activity
Recombinant Mouse TDO2 (Catalog # 10001-TD) is measured by its ability to oxidize L-tryptophan to N-formyl-kynurenine.
Recombinant Mouse TDO2 His-tag Protein SDS-PAGE
1 μg/lane of Recombinant Mouse TDO2 was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by silver staining, showing bands at 39 kDa and 75 kDa under R conditions.
Formulation, Preparation and Storage
What does CF mean?
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our
Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant
protein to be stored at a more dilute concentration.
The carrier free version does not contain BSA.
What formulation is right for me?
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or
as an ELISA standard.
In contrast, the carrier free protein is recommended for applications, in which the presence of BSA
Supplied as a 0.2 μm filtered solution in Tris, NaCl and Glycerol.
The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
6 months from date of receipt, -20 to -70 °C as supplied.
3 months, -20 to -70 °C under sterile conditions after opening.
Tryptophan 2,3-dioxygenase (TDO2), a heme-containing cytosolic dioxygenase, forms a homo-tetrameric active molecule of approximately 190 kDa composed of 48 kDa monomers (1, 2). Mouse TDO2 shares 89% aa sequence identity with human TDO2. TDO2 is one of three proteins capable of catalyzing the first and rate-limiting step of the L-kynurenine pathway (KP): oxidative cleavage of the essential amino acid L-tryptophan to form N formyl kynurenine (3). TDO2 is a cytosolic protein typically localized to the liver and brain, unlike the more ubiquitously expressed indoleamine 2,3-dioxygenase (IDO), yet it is responsible for ~90% of the primary route of catabolism of tryptophan through the KP (3). TDO2 is upregulated in extrahepatic tumors (4-6) and is consequently a target in cancer immunotherapy (7). TDO2 is a therapeutic target in brain disease such as schizophrenia, Alzheimers disease, multiple sclerosis and glioma (8-11) due to its role in the regulation of levels of critical biologically active downstream KP metabolites (3). Polymorphisms in the TDO2 gene have been implicated for a role in behavioural responses and autism (12,13).
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