Cat: PA1000-8395

Recombinant Human DEFb131 Protein,His

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Analytical Data

  • Gene name

    DEFb131

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    DEFb131;DEFB131;DEFB31;Beta-defensin 131A

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P59861

  • Expression Region

    23-70aa

  • AA Sequence

    FISNDECP SEYYHCRLKC NADEHAIRYC ADFSICCKLK IIEIDGQKKW

  • 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

The DEFb131 protein, a member of the defensin family, has garnered significant attention in the field of antimicrobial research due to its potent antibacterial and antifungal properties. Defensins are small cationic peptides found in various organisms, playing a crucial role in the innate immune response. The DEFb131 variant, specifically derived from plants, exhibits unique structural characteristics that enhance its stability and activity against a broad spectrum of pathogens. Recent studies have aimed to explore its protective mechanisms, focusing on its ability to disrupt microbial membranes and modulate immune responses. The increasing prevalence of antibiotic-resistant strains has underscored the urgency to investigate alternative antimicrobial agents, positioning DEFb131 as a promising candidate for the development of new therapeutic strategies. Furthermore, research has expanded to include its applications in agriculture, where it may provide a natural solution for crop protection against phytopathogens. As such, the study of DEFb131 is pivotal not only for understanding plant defense mechanisms but also for addressing the growing challenges posed by resistant infections in both human health and agricultural sustainability.

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