Cat: IPD-X40208

Recombinant Bacillus subtilis pbpE Protein ,His & SUMO

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Analytical Data

  • Gene name

    pbpE

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    PBP 4* Alternative name(s): PBP 4A Penicillin-binding protein E

  • Species

    Bacillus subtilis

  • Source

    E. coli

  • Tag

    N- His-SUMO

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P32959

  • Expression Region

    1-451aa

  • Molecular Weight

    67.4 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 recombinant protein pbpE is situated within the broader context of infectious disease research, particularly focusing on pathogens that exhibit antibiotic resistance. pbpE, which encodes a penicillin-binding protein in certain bacteria, plays a critical role in cell wall synthesis and maintenance, making it a key target for antibiotics. The emergence of resistant strains renders traditional antibiotic treatments less effective, highlighting the urgent need for new therapeutic strategies. Researchers are investigating pbpE not only to understand its structural and functional properties but also to explore its potential as a vaccine candidate or a therapeutic target. The recombinant expression of pbpE protein facilitates detailed analysis of its interactions and role in bacterial physiology, enabling the identification of novel inhibitors that could disrupt its function. Additionally, generating antibodies against pbpE might provide insights into immune responses to bacterial infections. Overall, this research focuses on harnessing the understanding of pbpE to combat antibiotic-resistant bacteria, which poses a significant threat to public health worldwide.

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