Cat: IPD-X37535

Recombinant Yersinia enterocolitica serotype O:8 Propionate kinase/TdcD Protein,His

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Analytical Data

  • Gene name

    Propionate kinase/TdcD

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Species

    Yersinia enterocolitica serotype O:8

  • Source

    E. coli

  • Tag

    N- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    A1JIM9

  • Expression Region

    1-406aa

  • Molecular Weight

    48.0 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

Propionate kinase, also known as TdcD, is an enzyme that plays a critical role in the metabolic pathway of propionate, a short-chain fatty acid that is important for various biological processes. It catalyzes the conversion of propionate into propionyl phosphate, which is an essential step in energy production, especially in anaerobic bacteria, where fermentation processes are key to survival. The study of TdcD has garnered attention due to its potential applications in biotechnology and medicine, particularly in metabolic engineering and the development of biosynthetic pathways for the production of valuable compounds. Understanding the structure and function of the recombinant TdcD protein can provide insights into its enzymatic mechanisms and regulatory roles. Furthermore, the manipulation of this enzyme may lead to advancements in microbial fermentation technologies, enhancing the efficiency of production systems that utilize propionate as a substrate. Due to the rising interest in sustainable production methods and the need for innovative solutions in bioengineering, research on propionate kinase/TdcD is significant for both academic and practical applications, paving the way for new strategies in the production of biofuels, bioplastics, and other industrially relevant biochemicals. Overall, delving into the properties and functionality of recombinant TdcD holds promise not only for understanding fundamental biochemical processes but also for advancing the field of synthetic biology.

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