Analytical Data
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Gene name
gtfB
- Application
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Alternative Names
(GTF-I)(Dextransucrase)(Sucrose 6-glucosyltransferase)
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Species
Streptococcus mutans serotype c
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Source
E. coli
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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
P08987
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Expression Region
426-597aa
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Molecular Weight
26.8 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
The study of GtfB recombinant protein has garnered significant attention due to its pivotal role in the synthesis of glucans, which are essential polysaccharides in various biological processes. GtfB, a glucosyltransferase enzyme produced by certain bacterial species, such as Streptococcus mutans, is known for its ability to catalyze the transfer of glucose units from sucrose to form α-1,3-glucans. These glucans are integral to biofilm formation, influencing dental caries and other microbial interactions. Research on GtfB not only aids in understanding the molecular mechanisms of biofilm development and pathogenicity but also holds potential for biotechnological applications, such as in the production of functional food ingredients and therapeutic agents. The recombinant expression of GtfB allows for the detailed study of its enzymatic activity, substrate specificity, and structural properties. Furthermore, elucidating the function and regulation of GtfB can lead to novel strategies for controlling biofilm-related diseases, making it a focus of interest for microbiologists and biochemists alike. By harnessing the insights gained from GtfB research, scientists aim to develop innovative approaches to manage and prevent microbial infections and enhance beneficial microbial interactions in various environments.
