Cat: IPD-X28648

Recombinant Others kshA Protein,Strep & His

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Analytical Data

  • Gene name

    kshA

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Species

    Others

  • Source

    E. coli

  • Tag

    Strep;His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P71875

  • Expression Region

    M1-H386

  • Protein Length

    Full Length

  • 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

The study of kshA recombinant protein is rooted in its significance in microbial metabolism and biochemical applications. KshA, a key enzyme in the degradation of steroid compounds, particularly in the catabolism of steroid hormones, plays a critical role in environmental bioremediation and natural steroid recycling processes. Its function is crucial for microorganisms that utilize steroids as a carbon and energy source. The recombinant production of kshA allows for detailed analysis of its enzymatic properties and substrate specificities, providing insights into its catalytic mechanisms. This research is particularly relevant in the fields of synthetic biology and biotechnology, where there is a growing interest in harnessing microbial enzymes for various industrial applications, including waste treatment and biofuel production. Understanding kshA can also lead to the development of novel approaches for the synthesis of valuable biochemicals. Moreover, studying this protein contributes to our broader understanding of microbial diversity and their metabolic capabilities, highlighting the potential of harnessing natural processes for sustainable development. As research progresses, recombinant kshA may also be explored for its therapeutic potential, given the increasing importance of steroid compounds in pharmaceuticals. Therefore, the exploration of kshA not only sheds light on fundamental biological processes but also opens avenues for innovative applications in environmental and industrial biotechnology.

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