Cat: IPD-X41330

Recombinant Podisus maculiventris Thanatin Protein ,His & KSI

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Analytical Data

  • Gene name

    Thanatin

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Species

    Podisus maculiventris

  • Source

    E. coli

  • Tag

    N- His-KSI

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P55788

  • Expression Region

    1-21aa

  • Molecular Weight

    17.8 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

Thanatin is a potent antimicrobial peptide derived from the Tobacco Hornworm, Manduca sexta, known for its ability to combat a wide range of pathogens, including bacteria, fungi, and viruses. It belongs to the group of insect defensins, which are crucial components of the innate immune system in insects. The unique structure of Thanatin, characterized by a conserved α-helical region, contributes to its effectiveness in disrupting microbial membranes. Recent research has focused on the recombinant expression of Thanatin in various host systems, such as bacteria and yeast, to facilitate its production and study. This approach allows for a more accessible and scalable method of obtaining the peptide for further investigations into its mechanisms of action and potential therapeutic applications. Given the rising problem of antibiotic resistance, Thanatin and its derivatives are being explored as alternatives or complementary treatments to conventional antibiotics. Studies have shown promising results regarding its efficacy against multidrug-resistant strains, making Thanatin a subject of interest in the development of novel antimicrobial agents. The ongoing research aims to optimize its production, understand its interaction with microbial targets, and evaluate its safety and effectiveness in clinical settings, positioning Thanatin as a potential key player in the fight against infectious diseases.

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