Cat: IPD-X39806

Recombinant Paracoccus denitrificans oxidoreductase Protein ,His & KSI

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Analytical Data

  • 基因名

    oxidoreductase

  • Application

    SPRMSTBLIITCELISA细胞实验药物筛选

  • 别名

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

  • 种属

    Paracoccus denitrificans

  • 表达系统

    E. coli

  • 标签

    N- His-KSI

  • 纯度

    Greater than 90% as determined by SDS-PAGE.

  • 蛋白编号

    P55932

  • 表达区间

    1-31aa

  • 分子量

    18.4 kDa

  • 内毒素

    < 1.0 EU per μg protein as determined by the LAL method.

  • 性状

    Freeze-dried powder

  • 缓冲液

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • 复溶方法

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • 个性化定制

    点位突变 标签定制 buffer定制 全长蛋白定制

  • 稳定性测试

    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.

  • 保存条件 & 期限

    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.

  • 运输条件

    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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IPODIX North America (HQ)
Proteintech Group, Inc
5500 Pearl Street, Suite 400
Rosemont, IL 60018, USA
1-888-478-4522
proteintech@ptglab.com
IPODIX North America (HQ)
Proteintech Group, Inc
5500 Pearl Street, Suite 400
Rosemont, IL 60018, USA
1-888-478-4522
proteintech@ptglab.com
IPODIX North America (HQ)
Proteintech Group, Inc
5500 Pearl Street, Suite 400
Rosemont, IL 60018, USA
1-888-478-4522
proteintech@ptglab.com
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