Cat: IPD-X40560

Recombinant Escherichia coli O157:H7 fadL Protein ,His & SUMO

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Analytical Data

  • Gene name

    fadL

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Outer membrane FadL protein Outer membrane flp protein

  • Species

    Escherichia coli O157:H7

  • Source

    E. coli

  • Tag

    N- His-SUMO

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q8XCN6

  • Expression Region

    26-446aa

  • Molecular Weight

    61.9 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 fadL gene, which encodes a protein involved in the transport of fatty acids across the outer membrane of Gram-negative bacteria, has garnered significant attention in the field of molecular biology and biotechnology. In recent years, researchers have focused on understanding the structure and function of the FadL protein, as it plays a crucial role in the utilization of fatty acids as carbon and energy sources. The interest in FadL stems from its potential applications in various industries, including bioremediation, biofuel production, and the development of novel antimicrobial strategies. The ability of FadL to facilitate the uptake of long-chain fatty acids makes it a valuable tool for engineering bacteria capable of degrading environmental pollutants or producing biofuels from waste materials. Studies have highlighted the importance of FadL in bacterial survival and growth in nutrient-limited environments, emphasizing its role in metabolic flexibility. Researchers employ techniques such as gene cloning, protein expression, and structural analysis to gain insights into the functional mechanisms of FadL and its interactions with fatty acids. Overall, the exploration of fadL recombinant protein contributes to our understanding of bacterial metabolism and opens up possibilities for innovative applications in biotechnology and environmental science.

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