Cat: IPD-X40500

Recombinant Lecanicillium psalliotae ver Protein ,His & Myc

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Analytical Data

  • Gene name

    ver

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Alkaline serine protease ver112; EC 3.4.21.-

  • Species

    Lecanicillium psalliotae

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q68GV9

  • Expression Region

    103-382aa

  • Molecular Weight

    36.0 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 research on verotoxin (VT) or Shiga toxin-producing Escherichia coli (STEC) proteins has gained prominence due to their significant impact on public health and food safety. Verotoxins, particularly VT1 and VT2, are potent exotoxins that can cause severe gastrointestinal diseases, including hemorrhagic colitis and hemolytic uremic syndrome (HUS), which can lead to kidney failure and death. These toxins are primarily associated with certain strains of E. coli, such as E. coli O157:H7. The molecular mechanisms through which verotoxins exert their harmful effects involve the inhibition of protein synthesis in host cells, leading to cell death and inflammatory responses. As outbreaks of STEC infections have been linked to contaminated food products, especially undercooked meat and unpasteurized dairy, understanding the structure and function of verotoxin proteins is crucial for developing effective diagnostic tools, vaccines, and targeted therapeutics. Recent advancements in structural biology and protein engineering have facilitated the elucidation of the mechanisms of action of these toxins, paving the way for potential strategies to mitigate their effects. Furthermore, the exploration of verotoxin protein analogs may provide insights into creating safer alternatives for therapeutic applications, highlighting the dual nature of these proteins in both pathogenesis and potential biomedical innovations.

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