Cat: IPD-X40324

Recombinant Escherichia coli lexA Protein ,His & SUMO

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Analytical Data

  • Gene name

    lexA

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    lexA; exrA; spr; tsl; umuA; b4043; JW4003LexA repressor; EC 3.4.21.88

  • Species

    Escherichia coli

  • Source

    E. coli

  • Tag

    N- His-SUMO

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P0A7C2

  • Expression Region

    1-202aa

  • Molecular Weight

    38.4 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 lexA gene, initially identified in Escherichia coli, encodes a regulatory protein that plays a crucial role in the bacterial SOS response to DNA damage. This protein functions as a transcription repressor, inhibiting the expression of various genes involved in DNA repair and maintenance under normal conditions. However, upon DNA damage, lexA undergoes auto-cleavage, leading to the activation of SOS genes that facilitate DNA repair processes. The study of lexA and its recombinant protein has garnered significant attention due to its implications in understanding bacterial stress responses, antibiotic resistance, and the modulation of gene expression in response to environmental challenges. Furthermore, the lexA repressor and its regulatory mechanisms have been utilized in synthetic biology for the development of gene regulation circuits, leveraging its ability to control gene expression in a precise and tunable manner. Research into lexA also extends to its potential applications in biotechnology and medicine, particularly in the development of novel antimicrobial strategies by targeting its functions. Overall, the lexA repressor serves as a fundamental model for investigating cellular responses to DNA damage and has important implications for both basic research and practical applications in microbial engineering and therapy.

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