Analytical Data
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Gene name
PAR2 Protein-VLP
- Application
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Alternative Names
GPR11; PAR2
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Species
Human
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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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Uniprot
P55085
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Expression Region
S37-Y397
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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
PAR2 protein, a member of the protease-activated receptor family, plays a crucial role in various physiological and pathological processes, including inflammation, pain, and cancer progression. Its activation by specific proteases leads to a cascade of signaling events that impact cellular behavior and immune responses. Recent studies have highlighted the potential of PAR2 as a therapeutic target, making the need for effective recombinant protein production increasingly important. Virus-like particles (VLPs) have emerged as a promising platform for the presentation of PAR2 protein due to their high stability, immunogenicity, and ability to mimic natural viral particles without containing viral genetic material. By utilizing VLPs, researchers can enhance the delivery and presentation of PAR2 epitopes, potentially leading to improved immune responses in vaccine development and targeted therapies. Moreover, the production of PAR2-containing VLPs allows for a better understanding of PAR2's role in cellular signaling and disease mechanisms. The combination of recombinant protein technology and VLP platforms offers innovative strategies for advancing PAR2-related research and therapeutic applications, opening new avenues in the study of extracellular signaling and its implications for human health.
