Cat: PA2000-4586

Recombinant Human ssuE Protein,His

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Analytical Data

  • Gene name

    ssuE

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    ssuE;ycbP;FMN reductase (NADPH)

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P80644

  • Expression Region

    1-191aa

  • AA Sequence

    MRVITLAGSPRFPSRSSSLLEYAREKLNGLDVEVYHWNLQNFAPEDLLYARFDSPALKTFTEQLQQADGLIVATPVYKAAYSGALKTLLDLLPERALQGKVVLPLATGGTVAHLLAVDYALKPVLSALKAQEILHGVFADDSQVIDYHHRPQFTPNLQTRLDTALETFWQALHRRDVQVPDLLSLRGNAHA

  • 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

The research on ssuE recombinant proteins is rooted in the growing interest in understanding the biochemical and physiological roles of sulfur metabolism in various organisms. The ssuE gene is part of the sulfur assimilation pathway, which is crucial for organisms to incorporate sulfur into essential biomolecules like amino acids and coenzymes. Studies have shown that ssuE encodes a protein involved in the conversion of sulfite to sulfide, a key step in this pathway. Investigating the recombinant form of ssuE provides insights into its enzymatic mechanisms, substrate specificity, and potential regulatory roles within the sulfur metabolism framework. Moreover, utilizing recombinant DNA technology allows for the expression and purification of the ssuE protein, facilitating detailed structural and functional analyses. This research not only enhances our understanding of microbial ecology and the sulfur cycle but also has implications for biotechnological applications, such as bioenergy production and bioremediation, where sulfur assimilation plays a vital role. By elucidating the properties and functions of ssuE recombinant proteins, scientists aim to develop novel strategies to manipulate sulfur metabolic pathways, potentially leading to advancements in environmental biotechnology and agricultural practices. Overall, the study of ssuE recombinant proteins represents a significant contribution to our comprehension of sulfur dynamics and its broader impacts on ecosystem health and sustainability.

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