Analytical Data
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Gene name
glucosyltransferase
- Application
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Species
Citrus unshiu
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Source
Baculovirus
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9MB73
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Expression Region
1-511aa
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Molecular Weight
61.4 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
Glucosyltransferases are a family of enzymes that catalyze the transfer of glucosyl groups from donor substrates, typically activated sugars like UDP-glucose, to various acceptor molecules. These enzymes play a crucial role in multiple biological processes, including carbohydrate metabolism, cell signaling, and the synthesis of polysaccharides. The study of glucosyltransferases has garnered significant interest due to their potential applications in biotechnology, medicine, and food industries. For instance, their ability to modify carbohydrate structures can be employed in the production of novel glycosylated compounds with enhanced properties, such as improved solubility, stability, and bioactivity. In the pursuit of understanding their structure-function relationships, researchers often employ recombinant DNA technology to produce glucosyltransferases in various host systems, enabling large-scale production and detailed biochemical characterization. The recombinant proteins allow for the exploration of enzyme specificity, kinetic properties, and the mechanism of glucosyl transfer, facilitating the development of tailored enzymes for industrial applications. Additionally, advances in structural biology have enabled the elucidation of the 3D structures of these enzymes, providing insights into their catalytic mechanisms and potential for engineering more efficient variants. As a result, the research on glucosyltransferase recombinant proteins holds promise not only for fundamental biological understanding but also for the innovation of sustainable bioprocesses in diverse fields.











