Analytical Data
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Gene name
NSP
- Application
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Alternative Names
SERPINI1; PI12; Serpin Peptidase Inhibitor Clade I Member 1; Peptidase inhibitor 12
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Species
Human
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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
Q99574
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Expression Region
Thr17~Leu410
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Molecular Weight
49kDa
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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
NSP (Nonstructural Proteins) in virology, particularly with regard to coronaviruses, play a crucial role in the viral life cycle, including replication, transcription, and immune evasion. The study of NSPs, especially NSP3 and NSP15, has garnered significant attention due to their multifunctional properties and potential as targets for therapeutic interventions. As researchers strive to understand the molecular mechanisms underlying viral pathogenesis, the recombinant expression of NSP proteins has become a pivotal area of focus. This is because recombinant NSP proteins can be utilized to elucidate their biological functions, assess their interaction with host cell machinery, and develop vaccines or antiviral drugs. Moreover, advancements in molecular biology techniques have facilitated the production of high-yield NSPs, enabling more sophisticated structural and functional analyses. The increasing prevalence of zoonotic diseases, exemplified by the recent COVID-19 pandemic, emphasizes the urgency for deeper insights into NSPs. Such research not only enhances our understanding of coronavirus biology but also informs the design of broad-spectrum antiviral strategies. Therefore, the exploration of NSP recombinant proteins is integral to advancing our knowledge of viral mechanisms and developing effective interventions in infectious diseases.
