Cat: IPD-X40187

Recombinant Halobacterium halobium bop Protein ,His & SUMO

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Analytical Data

  • Gene name

    bop

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    BR

  • Species

    Halobacterium halobium

  • Source

    E. coli

  • Tag

    N- His-SUMO & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P33972

  • Expression Region

    149-166aa

  • Molecular Weight

    18.0 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

Bop (Bacterial Outer Membrane Protein) is an essential protein found in the outer membrane of Gram-negative bacteria, playing a critical role in maintaining membrane integrity and facilitating nutrient transport. Research on Bop and its structural and functional characteristics has gained importance due to its potential applications in biotechnology and medicine. Understanding Bop's mechanism can lead to insights into bacterial pathogenesis and resistance, thereby aiding in the development of novel antibacterial agents. Furthermore, Bop is also being studied for its potential as a vaccine target, given that it is exposed on the bacterial surface, making it accessible to the host's immune system. Additionally, the ability to engineer Bop could open pathways for creating biosensors or drug delivery systems. Recent advances in recombinant DNA technology have made it easier to produce and purify Bop, leading to more detailed studies on its properties and interactions with other cellular components. The investigation of Bop not only deepens our knowledge of bacterial physiology but also contributes to overcoming the challenges posed by antibiotic resistance and infectious diseases. Overall, Bop research stands at the intersection of microbiology, structural biology, and therapeutic development, underscoring its significance in contemporary scientific inquiry.

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