Analytical Data
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Gene name
Varicella zoster virus
- Application
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Alternative Names
Glycoprotein E/gE (VZV)
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Species
Virus
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Source
HEK293
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Tag
C-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9J3M8-1
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Expression Region
S31-A546
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Protein Length
Partial
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Molecular Weight
54-69 kDa,based on SDS-PAGE under non-reduced conditions,due to the glycosylation.
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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
Varicella zoster virus (VZV) is a member of the Herpesviridae family and is responsible for causing chickenpox (varicella) in children and shingles (zoster) in adults. After initial infection, VZV remains dormant in the sensory neurons and can reactivate later in life, leading to painful zoster outbreaks. The development of effective vaccines and antiviral therapies is crucial for managing these conditions. In recent years, research has increasingly focused on the use of recombinant proteins derived from VZV to enhance immune responses. These recombinant proteins, which may include glycoproteins and other viral components, can serve as potential candidates for vaccine development or diagnostic assays. Understanding the immunogenic properties of these proteins can help in designing more effective vaccines that can elicit robust and long-lasting immunity. Additionally, recombinant protein studies can provide insights into the mechanisms of VZV pathogenesis and the host immune response, which are essential for developing targeted therapies. As such, the exploration of VZV recombinant proteins represents a promising avenue for advancing our strategies against VZV-related diseases, ultimately aiming to reduce the incidence and severity of varicella and zoster in populations worldwide.
