Cat: IPD-X40535

Recombinant Mouse Wdpcp Protein ,GST

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Analytical Data

  • Gene name

    Wdpcp

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Homolog-13WD repeat-containing and planar cell polarity effector protein

  • Species

    Mouse

  • Source

    E. coli

  • Tag

    N- GST

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q8C456

  • Expression Region

    1-722aa

  • Molecular Weight

    108.7 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

The study of WdpCp protein, a potential antimicrobial peptide derived from the bacterial species, has garnered significant attention in recent years due to its unique properties and applications in molecular biology and medicine. As antibiotic resistance becomes a pressing global health issue, researchers are exploring alternative strategies to combat bacterial infections. WdpCp, characterized by its ability to disrupt bacterial membranes, presents a promising avenue for developing new antimicrobial agents. Its structure and function have been investigated to understand the mechanisms underlying its antibacterial activity, which could lead to the design of more effective therapeutic agents. Moreover, the recombinant production of WdpCp in various expression systems allows for detailed analysis and offers the potential for large-scale production, overcoming the limitations associated with natural extraction. This research not only enhances our understanding of bacterial interactions but also aims to contribute to the development of innovative solutions in the fight against infectious diseases, making WdpCp a focal point in the search for novel antimicrobial strategies.

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