Cat: PA2000-2570

Recombinant E.coli bop Protein,His

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Analytical Data

  • Gene name

    bop

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    bop;BOP;C22orf29;Protein Bop

  • Species

    E.coli

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P33972

  • Expression Region

    149-166aa

  • AA Sequence

    SLSGRVANLPSDTRSTFK

  • 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 (Bcl-2 homologous antagonist/killer protein) is a pivotal protein implicated in apoptosis regulation and is part of the Bcl-2 family. The study of BOP and its role in cellular processes has garnered significant attention due to its potential implications in cancer biology, where aberrant regulation of apoptosis is a hallmark of tumorigenesis. Researchers have identified that BOP can interact with various proteins that either promote or inhibit cell death, thus influencing survival pathways in both normal and cancerous cells. Understanding the structural and functional aspects of BOP is crucial, as it may provide insights into novel therapeutic strategies for cancers characterized by dysregulated apoptosis. Recent advances in recombinant protein technology have enabled the production of BOP in heterologous systems, allowing researchers to explore its biochemical properties and interactions in greater detail. Furthermore, investigations into the post-translational modifications of BOP could unveil new layers of regulation that impact its function and stability. Ongoing studies aim not only to elucidate the mechanistic pathways involving BOP but also to assess its potential as a target for drug development, paving the way for innovative treatments that can restore normal apoptotic signaling in cancer cells.

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