Cat: PA2000-4278

Recombinant E.coli plnA Protein,His

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Analytical Data

  • Gene name

    plnA

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    plnA;Bacteriocin plantaricin-A

  • Species

    E.coli

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P80214

  • Expression Region

    26-48aa

  • AA Sequence

    AYSLQMGATAIKQVKKLFKKWGW

  • Molecular Weight

    18.7 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

PlnA, a class II bacteriocin produced by Lactococcus lactis, has garnered significant research interest due to its potential as a natural antibacterial agent. Bacteriocins are ribosomally synthesized peptides that exhibit antimicrobial properties against various pathogenic bacteria, making them valuable for food preservation and therapeutic applications. The unique structure and mechanism of PlnA highlight its ability to disrupt membrane integrity in target bacteria, prompting studies into its efficacy and safety for use in food systems. Additionally, genetic engineering approaches have been employed to enhance the yield and activity of PlnA, allowing for the optimization of fermentation processes and better understanding of its functional properties. As the demand for natural preservatives and alternatives to conventional antibiotics grows, the exploration of PlnA and its derivatives offers promising avenues for developing innovative solutions to combat bacterial infections and spoilage, thereby contributing to public health and food safety.

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