Cat: IPD-X41407

Recombinant Escherichia coli bioH Protein ,His & Myc

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Analytical Data

  • Gene name

    bioH

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    (Biotin synthesis protein BioH)(Carboxylesterase BioH)

  • Species

    Escherichia coli

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P13001

  • Expression Region

    1-256aa

  • Molecular Weight

    35.9 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.

Quality inspection process

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Protein Description

BioH, or biotin biosynthesis enzyme, is a crucial component in the microbial synthesis of biotin, a vital coenzyme involved in various biochemical pathways, including fatty acid synthesis, amino acid metabolism, and gluconeogenesis. The study of BioH recombinant proteins has gained significance due to their potential applications in biotechnology and medicine. Understanding the structure and function of BioH not only provides insights into biotin metabolism but also opens avenues for the development of biotin-rich supplements and therapeutic agents. Recent advancements in genetic engineering and protein expression systems have enabled the production of recombinant BioH with enhanced stability and activity, making it a valuable tool in research and industrial processes. This research is particularly relevant in the context of nutrient deficiencies and the need for biocompatible solutions in health and nutrition, underscoring the importance of BioH in both natural and engineered biological systems. As biotin serves as a cofactor for important enzymatic reactions, elucidating the mechanisms of BioH will contribute to our understanding of metabolic regulation and may lead to innovations in health-related applications, such as targeted nutrient delivery and the development of probiotics designed for optimal nutrient absorption in humans and animals.

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