Analytical Data
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Gene name
DENV2 Envelope
- Application
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Alternative Names
Core protein Protein prM Peptide pr Small envelope protein M
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Species
Dengue virus type 2
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Source
Yeast
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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
P29990
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Expression Region
281-775aa
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Molecular Weight
56.43 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
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Protein Description
Dengue virus (DENV) is a significant global health concern, responsible for millions of infections each year, particularly in tropical and subtropical regions. The virus exists in four serotypes, with DENV2 being one of the most widely researched due to its association with severe dengue cases. The envelope (E) protein of DENV is a key component in the virus's structure, playing a crucial role in viral entry into host cells and eliciting immune responses. Research on the recombinant Envelope protein from DENV2 has gained attention for its potential applications in vaccine development and diagnostics. By expressing the E protein in various systems, scientists aim to understand its immunogenic properties and determine how it interacts with host immune mechanisms. Furthermore, recombinant E proteins can be used to generate specific antibodies, which are essential for both therapeutic interventions and the development of serological assays. Investigating the structural and functional characteristics of the DENV2 Envelope protein can provide insights into the virus's pathogenesis and aid in the design of effective vaccines that elicit robust immune responses without causing disease enhancement. This research is critical in combating dengue fever and reducing the burden of this disease worldwide.
