Cat: IPD-X33158

Recombinant E.coli ygiS Protein,His & SUMO

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Analytical Data

  • Gene name

    ygiS

  • 简介

    The ygiS protein may be an important component of the deoxycholate transport system and play an important role in cellular responses to bile acid detergents, especially deoxycholate. Its absence leads to increased levels of intracellular deoxycholic acid, resulting in decreased cell growth. ygiS Protein, E.coli (His-SUMO) is the recombinant E. coli-derived ygiS protein, expressed by E. coli , with N-His, N-SUMO labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    ygiS; b3020; JW2988; Probable deoxycholate-binding periplasmic protein YgiS

  • Species

    E.coli

  • Source

    E. coli

  • Tag

    N-His;N-SUMO

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q46863

  • Expression Region

    A21-H535

  • AA Sequence

    ADVPANTPLAPQQVFRYNNHSDPGTLDPQKVEENTAAQIVLDLFEGLVWMDGEGQVQPAQAERWEILDGGKRYIFHLRSGLQWSDGQPLTAEDFVLGWQRAVDPKTASPFAGYLAQAHINNAAAIVAGKADVTSLGVKATDDRTLEVTLEQPVPWFTTMLAWPTLFPVPHHVIAKHGDSWSKPENMVYNGAFVLDQWVVNEKITARKNPKYRDAQHTVLQQVEYLALDNSVTGYNRYRAGEVDLTWVPAQQIPAIEKSLPGELRIIPRLNSEYYNFNLEKPPFNDVRVRRALYLTVDRQLIAQKVLGLRTPATTLTPPEVKGFSATTFDELQKPMSERVAMAKALLKQAGYDASHPLRFELFYNKYDLHEKTAIALSSEWKKWLGAQVTLRTMEWKTYLDARRAGDFMLSRQSWDATYNDASSFLNTLKSDSEENVGHWKNAQYDALLNQATQITDATKRNALYQQAEVIINQQAPLIPIYYQPLIKLLKPYVGGFPLHNPQDYVYSKELYIKAH

  • Protein Length

    Full Length of Mature Protein

  • 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.

Quality inspection process

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Protein Description

YgiS, a protein associated with various biological processes, has garnered attention in recent years due to its potential roles in bacterial physiology and virulence. Initially identified in certain pathogenic strains of bacteria, YgiS has been suggested to play a critical role in stress response and metabolic regulation. Researchers have been particularly interested in its structure-function relationships, as the protein appears to be involved in the modulation of signaling pathways essential for bacterial adaptation to environmental challenges. Investigations into the recombinant expression of YgiS have enabled scientists to explore its biochemical properties and interactions with other cellular components in detail. This research is crucial, as understanding YgiS may contribute to the development of novel therapeutic strategies against bacterial infections. The protein’s involvement in enzymatic activities and regulatory mechanisms positions it as a potential target for innovative drug design aimed at disrupting virulence factors in pathogenic microbes. Consequently, characterizing the YgiS recombinantly not only provides insights into its fundamental roles within microbial cells but also opens avenues for applied research in infectious disease management. As the field of protein engineering advances, efforts to elucidate the functional implications of YgiS could ultimately lead to breakthroughs in our understanding of microbial resilience and pathogenicity.

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