Cat: IPD-X41725

Recombinant Streptococcus mutans serotype c gtfC Protein ,His & Myc

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Analytical Data

  • Gene name

    gtfC

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    (GTF-SI)(Dextransucrase)(Sucrose 6-glucosyltransferase)

  • Species

    Streptococcus mutans serotype c

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P13470

  • Expression Region

    426-597aa

  • Molecular Weight

    26.7 kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • 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.

  • 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.

  • 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.

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Protein Description

GtfC, a crucial enzyme identified in the biosynthetic pathway of glucosyltransferases, plays a significant role in the production of exopolysaccharides in various microorganisms. These exopolysaccharides are important for their applications in food, pharmaceuticals, and biotechnology. Previous studies have indicated that GtfC is involved in the modification of polysaccharides, impacting their texture, viscosity, and functional properties. Researchers have focused on the recombinant expression of GtfC to explore its characteristics, optimize production processes, and comprehend its mechanisms of action. The recombinant protein offers a valuable model for elucidating the enzyme's structure-function relationship and for investigating its potential applications in industrial settings. With advancements in molecular biology techniques, including gene cloning and expression systems, scientists can produce GtfC in larger quantities, facilitating detailed biochemical studies and practical applications. Understanding GtfC's functionality not only sheds light on microbial polysaccharide synthesis but also opens up avenues for engineering enhanced strains for biotechnological purposes, such as improved fermentation processes or the development of novel materials with specific properties.

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