Cat: IPD-X40468

Recombinant Streptomyces sp. choA Protein ,GST

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Analytical Data

  • Gene name

    choA

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Cholesterol isomerase (EC:5.3.3.1)

  • Species

    Streptomyces sp.

  • Source

    E. coli

  • Tag

    N- GST

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P12676

  • Expression Region

    43-546aa

  • Molecular Weight

    81.9 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

ChoA (Choline/ethanolamine protein) is a significant protein involved in bacterial metabolism and has garnered attention for its role in choline and ethanolamine utilization. The study of ChoA is particularly relevant due to its implications in the pathogenicity of certain bacteria, as it facilitates the utilization of these compounds as carbon and nitrogen sources, thereby enhancing bacterial survival in nutrient-limited environments. Furthermore, ChoA is crucial in understanding bacterial adaptability and resistance mechanisms, particularly in the context of biofilm formation and antibiotic resistance. The exploration of ChoA has also opened avenues for biotechnological applications, such as the development of microbial processes for choline and ethanolamine production, which are valuable in the pharmaceutical and food industries. By characterizing the structural and functional aspects of ChoA, researchers aim to elucidate its mechanism of action, paving the way for potential therapeutic targets against pathogenic bacteria that exploit this metabolic pathway. Overall, ongoing research on ChoA not only enhances our understanding of bacterial physiology but also contributes to the broader field of microbial ecology and biotechnology.

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