Cat: IPD-X39806

Recombinant Paracoccus denitrificans oxidoreductase Protein ,His & KSI

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Analytical Data

  • Gene name

    oxidoreductase

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Electron-transferring-flavoprotein dehydrogenase (ETF dehydrogenase ) (ETF-QO) (ETF-ubiquinone oxidoreductase)

  • Species

    Paracoccus denitrificans

  • Source

    E. coli

  • Tag

    N- His-KSI

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P55932

  • Expression Region

    1-31aa

  • Molecular Weight

    18.4 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

Oxidoreductases are a diverse class of enzymes that catalyze oxidation-reduction reactions, playing critical roles in various biological processes, including metabolism, cellular respiration, and detoxification. These enzymes facilitate the transfer of electrons between molecules, making them essential for energy production and the maintenance of cellular redox balance. The study of oxidoreductases has gained significant attention in recent years due to their potential applications in biotechnology, pharmacology, and environmental remediation. Recombinant protein technology has revolutionized the characterization and functional analysis of these enzymes by allowing for the production of large quantities of pure, active proteins. By cloning the genes encoding oxidoreductases into suitable expression systems, researchers can investigate their enzymatic properties, substrate specificities, and reaction mechanisms. Additionally, the manipulation of these enzymes through techniques such as site-directed mutagenesis can lead to improved catalysts for industrial processes or the development of novel therapeutic agents. Understanding the structure-function relationships of oxidoreductases through techniques like X-ray crystallography and NMR spectroscopy has also provided insights into their catalytic mechanisms and stability, further enhancing their applicability in various fields. Overall, the research on recombinant oxidoreductases represents a promising frontier in enzyme engineering and biocatalysis, with the potential to address challenges in energy conversion, waste management, and drug development.

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