Cat: IPD-X40463

Recombinant Apis mellifera carnica Icarapin Protein ,His & Myc

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Analytical Data

  • Gene name

    Icarapin

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Venom protein 2 Allergen: Api m 10

  • Species

    Apis mellifera carnica

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q5EF78

  • Expression Region

    20-223aa

  • Molecular Weight

    27.7 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

Icarapin, a recombinant protein derived from the venom of the Chinese red-headed centipede (Scolopendra subspinipes), has garnered significant attention in biomedical research due to its potential therapeutic applications. Centipede venom is known for its complex mixture of bioactive compounds, which have evolved to possess various pharmacological properties, including antimicrobial, anti-inflammatory, and analgesic effects. The interest in Icarapin is primarily driven by its unique ability to modulate immune responses and its potential to act as an immunomodulatory agent. Studies have demonstrated that Icarapin can interact with immune cells, potentially enhancing their function and promoting the body’s defense mechanisms against infections. Furthermore, its recombinant form allows for more controlled studies, as well as the possibility of large-scale production, which is crucial for clinical applications. As researchers continue to explore the mechanism of action and the therapeutic potential of Icarapin, it could pave the way for novel treatments in infectious diseases, autoimmune disorders, and other conditions where immune regulation is critical. This makes Icarapin a promising candidate in the field of biopharmaceuticals, with the potential to address unmet medical needs through innovative therapeutic strategies.

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