SARS Nucleocapsid, 1-49 a.a.
Protein is >90% pure as determined SDS-PAGE.
Description
The E.coli derived recombinant protein contains the Nucleocapsid protein 1-49 amino acids immunodominant regions.
Product Specs
The SARS Nucleocapsid protein plays a vital structural role in the virus. It binds with the RNA genome, forming a helical nucleocapsid. This protein comprises three structural domains and is associated with three outer structural proteins: membrane (M), envelope (E), and spike (S) proteins.
This recombinant protein is derived from E. coli and encompasses amino acids 1 to 49 of the Nucleocapsid protein, representing immunodominant regions.
The SARS Nucleocaspid protein solution is supplied in a phosphate-buffered saline (PBS) solution.
The protein is shipped with ice packs to maintain a low temperature. Upon receiving, store the protein at -20 degrees Celsius.
SDS-PAGE analysis confirms that the protein purity is greater than 90%.
Purified by proprietary chromatographic technique.
Immunoreactive with sera of SARS-infected individuals.
Product Science Overview
The Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) nucleocapsid protein is a crucial component of the virus’s structure and function. The recombinant form of the nucleocapsid protein, specifically the first 49 amino acids (1-49 a.a.), has been extensively studied for its role in the viral life cycle and its potential applications in diagnostics and therapeutics.
The nucleocapsid (N) protein of SARS-CoV is a highly conserved structural protein that plays a pivotal role in the packaging of the viral RNA genome into ribonucleoprotein complexes. This protein is essential for the assembly and release of new virions. The N protein is composed of multiple domains, each contributing to its function:
- N-terminal domain (NTD): This domain, which includes the first 49 amino acids, is responsible for RNA binding and is crucial for the formation of the ribonucleoprotein complex.
- C-terminal domain (CTD): This domain is involved in dimerization and interaction with other viral and host proteins.
The N protein is involved in several key processes during the SARS-CoV life cycle:
- RNA Binding: The NTD binds to the viral RNA genome, facilitating its encapsidation into ribonucleoprotein complexes.
- Virion Assembly: The N protein interacts with the membrane (M) protein to drive the assembly of new virions.
- Host Interaction: The N protein can modulate host cell processes, including the immune response, to enhance viral replication and evade host defenses.
The recombinant form of the N protein, particularly the first 49 amino acids, has been produced and studied for various applications:
- Diagnostics: The recombinant N protein can be used as an antigen in serological assays to detect antibodies against SARS-CoV in patient samples. This is crucial for diagnosing past infections and monitoring immune responses.
- Vaccine Development: The N protein is a target for vaccine development due to its high immunogenicity. Recombinant N protein-based vaccines aim to elicit a strong immune response against the virus.
- Therapeutics: Understanding the structure and function of the N protein can aid in the development of antiviral drugs that target its interactions with viral RNA and other proteins.
Recent studies have highlighted the importance of the N protein in the context of the SARS-CoV-2 pandemic. The N protein of SARS-CoV-2 shares significant similarity with that of SARS-CoV, making it a valuable target for cross-reactive diagnostics and therapeutics . Research has focused on the following areas:
- Structural Analysis: Detailed structural studies of the N protein have provided insights into its RNA-binding mechanisms and interactions with other viral proteins .
- Functional Studies: Functional analyses have identified key residues and domains critical for the N protein’s role in the viral life cycle .
- Vaccine and Drug Development: The N protein is being explored as a target for novel vaccines and antiviral drugs aimed at preventing and treating SARS-CoV-2 infections .
