Cat: IPD-X41505

Recombinant Bothrops asper BaP Protein ,His & Myc

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Analytical Data

  • Gene name

    BaP

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    (SVMP)(Hemorrhagic metalloproteinase BaP1)(Bap-1)

  • Species

    Bothrops asper

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P83512

  • Expression Region

    192-394aa

  • Molecular Weight

    30.3 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.

Quality inspection process

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Protein Description

The study of BaP (benzo[a]pyrene) recombinant proteins is rooted in the need to understand the effects of polycyclic aromatic hydrocarbons (PAHs) on human health and the environment. BaP, a well-known carcinogen produced through incomplete combustion of organic materials, poses significant risks through environmental exposure, particularly in urban areas and places with industrial activity. Research has shown that BaP can induce various biological responses, including mutations and disruption of cellular processes, raising concerns about its role in cancer development. Recombinant proteins, derived from genetically engineered organisms, play a crucial role in elucidating the molecular mechanisms of BaP toxicity and its interactions with biological systems. By utilizing these proteins, scientists can investigate the metabolic pathways, enzymatic activities, and genetic responses associated with BaP exposure. Moreover, the development of recombinant protein-based assays holds potential for bioremediation efforts and the detection of BaP in environmental samples. Understanding the structure-function relationship of BaP-related proteins through recombinant technologies can facilitate the identification of biomarkers for exposure and susceptibility, contributing to public health strategies and regulatory policies aimed at minimizing the risks associated with this hazardous compound.

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