Analytical Data
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Gene name
thiO
- Application
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Alternative Names
thiO; goxB; yjbR; BSU11670Glycine oxidase; GO; EC 1.4.3.19
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Species
Bacillus subtilis
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O31616
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Expression Region
1-369aa
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Molecular Weight
56.9 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
ThiO recombinant protein, derived from the thiocinase family, has garnered significant attention in recent years due to its potential applications in biocatalysis and biotechnology. The thiocinase enzymes are characterized by their ability to catalyze the cleavage of thioether bonds, which are prevalent in various substrates, including natural products and synthetic compounds. Research into ThiO aims to elucidate its biochemical properties, substrate specificity, and mechanistic pathways. This understanding could lead to novel applications in the synthesis of fine chemicals, pharmaceuticals, and agrochemicals. Additionally, the ability to engineer ThiO for enhanced stability and activity opens avenues for industrial applications, making it a target of interest for sustainable chemistry. Advances in recombinant DNA technology also facilitate the production of this enzyme in various host systems, improving yields and enabling large-scale applications. As such, the study of ThiO and its recombinant variants could significantly contribute to the fields of enzymology, green chemistry, and biotechnological innovation.
