Analytical Data
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Gene name
NA/Neuraminidase
- Application
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Species
Influenza A virus
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O91745
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Expression Region
31-469aa
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Molecular Weight
56.2 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
Neuraminidase (NA) is a crucial enzyme on the surface of influenza viruses, playing a significant role in the virus's lifecycle by facilitating the release of newly formed viral particles from infected cells and promoting viral spread. Its importance in the pathology of influenza has made NA a target for antiviral drugs, such as oseltamivir (Tamiflu) and zanamivir (Relenza), which inhibit its activity to reduce virus transmission. Furthermore, NA is also a key component in the development of influenza vaccines, particularly for its ability to elicit an immune response. Due to the frequent mutations in the NA gene, which can lead to variations in enzyme structure and function, continual surveillance and study of this protein are essential. The production of recombinant NA protein has gained traction as a valuable tool for research purposes. By utilizing techniques such as recombinant DNA technology, scientists can produce large quantities of pure NA for structural studies, functional assays, and vaccine development. This approach allows for a better understanding of the evolutionary dynamics of the virus and the immune response it elicits, providing insights into potential vaccine strategies and antiviral treatments. As influenza remains a significant global health challenge, ongoing research into NA recombinants aims to improve therapeutic options and guide public health responses to influenza outbreaks.
