Analytical Data
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Gene name
HEV1
- Application
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Alternative Names
Major hevein
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Species
Hevea brasiliensis
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P02877
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Expression Region
18-204aa
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Molecular Weight
24.1 kDa
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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
HEV1 recombinant protein research has gained significant attention due to its potential implications in vaccine development and therapeutic applications. The hepatitis E virus (HEV), a major cause of viral hepatitis worldwide, has been linked to both acute and chronic liver disease, particularly in immunocompromised individuals. As conventional vaccine strategies have had limited success against HEV, the production of recombinant proteins like HEV1 has emerged as a promising alternative. HEV1, derived from the ORF2 protein of the virus, plays a critical role in eliciting an immune response, making it a suitable candidate for further investigation. Recent studies have focused on optimizing the expression systems used for HEV1 production, enhancing its yield and stability, and evaluating its immunogenic properties through preclinical models. Understanding the structure and function of HEV1 is crucial for designing effective vaccines and treatments, which may mitigate the public health burden posed by HEV infections. Furthermore, advancements in protein engineering and adjuvant technologies could significantly improve the efficacy of HEV-based immunotherapies, paving the way for novel solutions to combat this resilient virus. As a result, researchers are increasingly exploring the potential of HEV1 recombinant protein not only for vaccine development but also for diagnostic applications, contributing to a comprehensive approach to managing HEV-related diseases.
