Analytical Data
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Gene name
Virus-Like Particles (VLPs) isotype control
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简介
Virus-Like Particles (VLPs) isotype control Protein (HEK293) is recommended for the control of CD133/PROM1 Protein-VLP, Human (HEK293, His) (HY-P78732), Claudin-3/CLDN3 Protein-VLP, Human (HEK293, His)(HY-P700472), Claudin-4/CLDN4 Protein-VLP, Human (HEK293, His)(HY-P700405), etc. For more control information on other VLP proteins, please refer to the description of the specific protein.
- Application
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Alternative Names
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Species
Virus
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Source
HEK293
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Molecular Weight
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
Related Products
Protein Description
Virus-like particles (VLPs) have emerged as a crucial platform in vaccine development and therapeutic protein applications due to their ability to mimic the structure and function of real viruses without containing any viral genetic material. This characteristic enables VLPs to elicit strong immune responses that are pivotal in protective immunity. The research surrounding VLPs isotype control recombinant proteins focuses on the manipulation of these particles to produce specific isotypes of antibodies that can enhance the clarity and specificity of immune responses in various applications. By engineering VLPs to express different isotypes, researchers aim to fine-tune the immune response, offering greater insights into the mechanisms of vaccine efficacy and the nature of antibody interactions. These engineered VLPs can serve as powerful tools for studying disease mechanisms and developing targeted therapies, paving the way for improved vaccines against infectious diseases and cancer. As the scientific community strives to optimize VLP design, understanding the role of antibody isotypes in the context of VLP-based vaccines becomes essential for advancing immunological research and therapeutic strategies.
