Cat: IPD-X40122

Recombinant Conus vexillum VxXXC Protein ,His & SUMO

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Analytical Data

  • Gene name

    VxXXC

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    VxXIIC

  • Species

    Conus vexillum

  • Source

    E. coli

  • Tag

    N- His-SUMO & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P0C1W7

  • Expression Region

    1-47aa

  • Molecular Weight

    25.3 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.

Quality inspection process

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Protein Description

VxXXC is a recombinant protein that has garnered significant attention in the field of immunology and vaccine development. Its design is rooted in the necessity to enhance immune responses against various pathogens, particularly in the context of emerging infectious diseases. With the increasing global burden of viral infections and the limitations of traditional vaccine platforms, researchers have focused on engineered proteins that can elicit robust immune responses. The VxXXC protein structure incorporates elements that promote better antigen presentation and stimulate both humoral and cellular immunity. Previous studies have suggested that recombinant proteins such as VxXXC can be tailored to improve stability and efficacy, making them suitable candidates for vaccines and therapeutics. The ongoing research aims to elucidate the mechanisms by which VxXXC functions, exploring its interactions with immune cells and the resulting modulation of immune pathways. This background underscores the potential of VxXXC in the advancement of next-generation vaccines that are not only effective but also safe and adaptable to the rapidly changing landscape of global health threats.

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