Cat: PA2000-2818

Recombinant E.coli lptC Protein,His

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Analytical Data

  • Gene name

    lptC

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    lptC;yrbK;Lipopolysaccharide export system Protein LptC

  • Species

    E.coli

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P0ADW0

  • Expression Region

    1-191aa

  • AA Sequence

    MSKARRWVIIVLSLAVLVMIGINMAEKDDTAQVVVNNNDPTYKSEHTDTLVYNPEGALSYRLIAQHVEYYSDQAVSWFTQPVLTTFDKDKIPTWSVKADKAKLTNDRMLYLYGHVEVNALVPDSQLRRITTDNAQINLVTQDVTSEDLVTLYGTTFNSSGLKMRGNLRSKNAELIEKVRTSYEIQNKQTQP

  • Molecular Weight

    23.7 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

LptC is a crucial protein involved in the assembly and transport of lipopolysaccharides (LPS) in Gram-negative bacteria, which play a vital role in the structural integrity of the bacterial outer membrane and are key determinants of bacterial virulence. The study of LptC and its function has garnered significant interest due to the increasing prevalence of antibiotic resistance in Gram-negative pathogens, which poses a serious threat to public health. Understanding the mechanisms underlying LPS biogenesis and the role of LptC can aid in the development of novel antibiotic strategies that target this essential process. Recent advances in recombinant DNA technology have enabled the expression and purification of recombinant LptC, which can be utilized for structural and functional analyses. Investigating the interactions of LptC with other components of the LPS transport machinery provides insights into its role in the overall assembly line of lipopolysaccharide synthesis and transport. Moreover, elucidating the structure-function relationship of LptC may reveal potential targets for inhibitors that could disrupt LPS transport, leading to increased susceptibility of pathogenic bacteria to antibiotics. Consequently, research on LptC as a model system not only contributes to our fundamental understanding of bacterial physiology but also holds promise for the development of new therapeutic strategies to combat multi-drug resistant infections.

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