Analytical Data
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Gene name
N354D,D364Y
- Application
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Alternative Names
S glycoprotein;E2;Peplomer protein
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Species
SARS-CoV-2
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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
P0DTC2
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Expression Region
319-541aa (N354D,D364Y)
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Molecular Weight
30.1 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
The N354D and D364Y mutations in proteins, particularly in the context of viral pathogens such as the human immunodeficiency virus (HIV), have garnered significant research interest due to their potential impact on viral replication and resistance to antiretroviral therapies. These specific amino acid substitutions can influence the structure and function of the viral enzymes and proteins, potentially altering their interaction with host cell machinery and mediating escape from immune responses or treatment regimens. The N354D mutation is often associated with increased replication capacity in certain strains, while D364Y has been linked to resistance against specific classes of drugs. Understanding the biochemical mechanisms underlying these mutations is crucial for developing effective therapeutics and vaccines. Researchers employ various techniques, including site-directed mutagenesis, protein expression, and functional assays, to investigate the consequences of these mutations on protein function and viral fitness. This research is vital for informing clinical strategies and enhancing our knowledge of viral evolution and resilience, ultimately contributing to improved management of HIV infections and potential cross-applicability to other viral systems.
