Cat: IPD-X41432

Recombinant Escherichia coli ssuE Protein (Baculovirus),His

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Analytical Data

  • Gene name

    ssuE

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    (NADPH)(FMN reductase)(Sulfate starvation-induced protein 4)(SSI4)

  • Species

    Escherichia coli

  • Source

    Baculovirus

  • Tag

    C- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P80644

  • Expression Region

    1-191aa

  • Molecular Weight

    26.9 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.

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Protein Description

ssuE, a gene coding for the ssuE protein, has garnered research interest due to its pivotal role in sulfur metabolism within various microorganisms. This protein is part of the sulfate assimilation pathway, which is crucial for organisms that rely on sulfate as a sulfur source. Understanding the function and regulation of ssuE can shed light on the complex biochemical processes that enable these organisms to thrive in sulfur-limited environments. The significance of ssuE extends beyond microbial ecology; it is also relevant in biotechnological applications, such as bioleaching and bioremediation, where sulfur compounds play a critical role. Recent studies have aimed to characterize the biochemical properties of the ssuE protein, including its enzymatic activity, structural features, and interactions with other cellular components. By utilizing advanced techniques such as recombinant protein expression and purification, researchers have begun to elucidate the detailed mechanisms by which ssuE functions in sulfur assimilation. This research not only enhances our understanding of microbial physiology but also has implications for environmental sciences and industrial biotechnology, where optimizing sulfur-related processes can lead to more sustainable practices. Thus, the study of ssuE and its recombinant protein forms represents a promising avenue for both basic and applied research in microbiology and biochemistry.

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