Analytical Data
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Gene name
NSP5
- Application
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Alternative Names
3C-like proteinase
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Species
SARS-CoV-2
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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
P0DTD1/YP_009725301.1
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Expression Region
1-306aa
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Molecular Weight
39.8 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
NSP5, or Non-structural Protein 5, is a crucial component in the life cycle of various coronaviruses, including SARS-CoV and SARS-CoV-2. As an important protease, NSP5 is responsible for processing viral polyproteins, which are essential for viral replication and assembly. The study of NSP5 recombinant protein has garnered significant attention due to its potential as a target for antiviral drug development and vaccine design. Understanding the structure and enzymatic function of NSP5 can provide critical insights into its role in viral pathogenesis and the host immune response. Moreover, the recombinant expression of NSP5 facilitates the investigation of its interactions with other viral and host proteins, potentially uncovering novel therapeutic strategies. Recent advances in molecular biology and protein engineering techniques have enabled researchers to produce NSP5 in various expression systems, allowing for comprehensive biochemical characterization and functional studies. Given the ongoing global challenges posed by coronaviruses, NSP5 remains a focal point in virology research, with implications for public health and disease control strategies.
