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View ProductsSize | 100ug, 50ug |
---|---|
Brand | ProteoGenix |
Product type | COVID-19 products |
Host Species | Escherichia coli (E. coli) |
Product name | NSP15 |
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Origin species | SARS-COV2 |
Expression system | Prokaryotic expression |
Molecular weight | 41,2kDa |
Purity estimated | 80% |
Buffer | PBS, pH7.5, 0.02%NLS |
Form | liquid |
Delivery condition | Dry Ice |
Storage condition | 4°C for short term; -20°c or -80°C for long term |
Brand | ProteoGenix |
Host species | Escherichia coli (E.coli) |
Fragment Type | Full length |
Aliases /Synonyms | Nidoviral RNA uridylate-specific endoribonuclease |
Reference | PX-COV-P030 |
Note | For research use only |
NSP15, also known as non-structural protein 15, is a viral protein found in coronaviruses, including the current pandemic-causing virus, SARS-CoV-2. This protein plays a crucial role in the replication and assembly of the virus, making it an important target for research and potential therapeutic interventions. In this article, we will discuss the structure, activity, and potential applications of NSP15 in the context of viral proteins, COVID antigens, and antibodies.
NSP15 is a multi-domain protein consisting of 346 amino acids, with a molecular weight of approximately 40 kDa. It is composed of three distinct domains: an N-terminal domain, a central domain, and a C-terminal domain. The N-terminal domain is responsible for binding to RNA, while the central domain contains the catalytic site for the protein’s enzymatic activity. The C-terminal domain is involved in protein-protein interactions and plays a role in the protein’s oligomerization. The overall structure of NSP15 is highly conserved among coronaviruses, making it a potential target for broad-spectrum antiviral therapies.
NSP15 is a highly conserved endoribonuclease, meaning it has the ability to cleave RNA molecules at specific sites. This activity is essential for the replication and assembly of the virus, as it allows the virus to hijack the host cell’s machinery and produce more viral particles. NSP15 specifically targets double-stranded RNA, which is a common intermediate in the replication process of coronaviruses. By cleaving these RNA molecules, NSP15 helps to prevent the host cell from producing interferons, which are proteins that can inhibit viral replication. This activity also helps the virus to evade the host immune response, making NSP15 an important factor in the pathogenesis of COVID-19.
Due to its crucial role in viral replication and assembly, NSP15 has been identified as a potential target for antiviral therapies. Several studies have shown that inhibiting NSP15’s enzymatic activity can significantly reduce viral replication and decrease the severity of COVID-19 symptoms. One study found that a small molecule inhibitor of NSP15 was effective in reducing viral load and lung damage in a mouse model of COVID-19. This suggests that targeting NSP15 could be a promising strategy for the development of antiviral drugs against SARS-CoV-2.
In addition to its potential as a therapeutic target, NSP15 is also being studied as a potential diagnostic tool. Antibodies against NSP15 have been shown to be present in the blood of individuals infected with SARS-CoV-2, indicating that NSP15 could be used as an antigen in serological tests for COVID-19. This could provide a more accurate and reliable method for detecting past infections and monitoring the spread of the virus.
NSP15 is a crucial viral protein found in coronaviruses, including the current pandemic-causing virus, SARS-CoV-2. Its structure, activity, and potential applications make it a key target for research and therapeutic interventions. As we continue to learn more about the role of NSP15 in COVID-19, it is likely to play an important role in the development of treatments and diagnostic tools for this ongoing global health crisis.
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