Cat: IPD-X29883

Recombinant Virus Virus-Like Particles (VLPs) isotype control Protein (HEK293)

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Analytical Data

  • Gene name

    Virus-Like Particles (VLPs) isotype control

  • 简介

    Virus-like particle (VLP) protein isotype controls, self-assembled from viral envelope or capsid proteins, serve as controls for displaying membrane proteins. Formed in HEK293 cell cultures, VLPs concentrate membrane proteins on the cell surface, creating high-concentration proteins ideal for immunization and antibody screening.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Species

    Virus

  • Source

    HEK293

  • Tag

    Tag Free

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • 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

Virus-Like Particles (VLPs) have emerged as a promising platform for vaccine development and immunotherapy due to their ability to mimic the structure of real viruses without containing viral genetic material. These particles can elicit strong immune responses, making them ideal candidates for antigen delivery. In research involving VLPs, isotype control recombinant proteins play a crucial role in validating experimental results, particularly in immunological assays. Isotype controls are antibodies of the same species and subclass as the test antibodies, which lack specific binding to the target antigen. In studies utilizing VLPs, these controls help ensure that observed immune responses are indeed due to the specific interactions with the VLPs rather than non-specific binding or background noise. The development of isotype control VLPs allows researchers to systematically assess the efficacy and specificity of the immune response elicited by VLP-based vaccines or therapies. As VLP technology advances, understanding the nuanced interactions between VLPs and the immune system becomes essential for optimizing their design and improving vaccine efficacy. This focus on isotype controls ultimately enhances the reliability and interpretability of findings in the burgeoning field of VLP research, paving the way for innovative applications in disease prevention and treatment.

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