Cat: IPD-X40097

Recombinant Escherichia coli yegS Protein ,His & SUMO

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Analytical Data

  • Gene name

    yegS

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    yegS; b2086; JW2070; Lipid kinase YegS; EC 2.7.1.-

  • Species

    Escherichia coli

  • Source

    E. coli

  • Tag

    N- His-SUMO

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P76407

  • Expression Region

    1-299aa

  • Molecular Weight

    48 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 yegS gene, found in various bacteria including Escherichia coli, encodes a protein that is believed to play a role in cellular processes such as stress response and metabolism. Recent studies have indicated that yegS may influence bacterial growth and survival under stressful conditions, making it an attractive target for further investigation. Researchers are particularly interested in understanding the function of the yegS protein and its potential applications in biotechnology and medicine. Recombinant expression of yegS protein allows scientists to produce large quantities of the protein for in vitro studies, facilitating detailed functional assays and structural analysis. Understanding the molecular mechanisms behind yegS activity may provide insights into bacterial adaptability and resilience, which could inform the development of new antimicrobial strategies or industrial applications. Furthermore, exploring the evolutionary conservation of yegS across different species could shed light on its fundamental biological role, highlighting its importance in the broader context of microbial physiology. As such, yegS represents a promising candidate for studies aimed at deciphering bacterial responses to environmental challenges, with potential implications for enhancing therapeutic approaches or engineering microbial strains with improved performance in various industries. Overall, the investigation of yegS recombination protein stands at the intersection of microbiology, genetics, and biotechnology, paving the way for innovations that harness the capabilities of microbes in diverse fields.

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