SARS Nucleocaspid (2-422), HEK
HEK293
Protein is >85% pure as determined SDS-PAGE.
Description
The HEK293 derived recombinant protein contains the SARS Coronavirus Nucleoprotein, amino acids 2-422 fused to a 6 His tag at N-terminal.
Product Specs
The SARS Coronavirus, an enveloped virus, possesses three key structural proteins on its exterior: membrane (M), envelope (E), and spike (S) proteins. The spike (S) glycoprotein facilitates viral entry into host cells by binding to a cellular receptor and mediating membrane fusion. Therefore, the S-protein is crucial for the virus's infection cycle and serves as the primary target for neutralizing antibodies.
This recombinant protein, derived from HEK293 cells, comprises the SARS Coronavirus Nucleoprotein (amino acids 2-422) with a 6-His tag fused to its N-terminal end.
The SARS Nucleocapsid protein solution is supplied in a solution containing 0.28M NaCl and 50mM HEPES at a pH of 8.0.
The SARS nucleoprotein is shipped with ice packs to maintain its temperature. Upon receipt, it should be stored at -20 degrees Celsius.
SDS-PAGE analysis indicates that the protein purity is greater than 85%.
HEK293
Purified by immobilized metal affinity chromatographic technique.
Product Science Overview
The Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) is the virus responsible for the COVID-19 pandemic. Among its structural proteins, the nucleocapsid (N) protein plays a crucial role in the viral life cycle. The recombinant form of this protein, expressed in Human Embryonic Kidney (HEK) cells, is widely used in research and diagnostic applications.
The nucleocapsid protein of SARS-CoV-2 is a highly conserved structural protein involved in several key processes of the viral life cycle, including viral RNA packaging, replication, and transcription . It is composed of 419 amino acids and has a molecular weight of approximately 45.6 kDa . The protein is known for its high immunogenicity, making it a prime target for diagnostic assays and potential therapeutic interventions .
Structure and Function
The N protein is divided into two major domains: the N-terminal RNA-binding domain (NTD) and the C-terminal dimerization domain (CTD). These domains are connected by a flexible linker region rich in serine and arginine residues . The NTD is responsible for binding to the viral RNA genome, while the CTD facilitates the dimerization and oligomerization of the protein, which is essential for the formation of the ribonucleoprotein complex .
The N protein also undergoes various post-translational modifications, including phosphorylation, which regulate its function and interactions with other viral and host proteins . Additionally, the N protein is involved in the modulation of the host cell’s immune response, further highlighting its importance in the viral life cycle .
Human Embryonic Kidney (HEK) 293 cells are a widely used mammalian cell line for the production of recombinant proteins . These cells were originally derived from human embryonic kidney cells and have been extensively utilized in research due to their high transfectivity, rapid growth rate, and ability to produce proteins with human-like post-translational modifications .
Advantages of HEK 293 Cells
- High Transfectivity: HEK 293 cells are highly amenable to transfection, allowing for efficient introduction of foreign DNA and subsequent protein expression .
- Human-like Post-translational Modifications: Proteins expressed in HEK 293 cells undergo post-translational modifications similar to those in human cells, ensuring proper folding and functionality .
- Rapid Growth: These cells grow quickly and can be cultured in both adherent and suspension conditions, making them suitable for large-scale protein production .
The recombinant SARS-CoV-2 nucleocapsid protein expressed in HEK 293 cells is used in various applications, including:
- Diagnostic Assays: The high immunogenicity of the N protein makes it an ideal target for serological assays to detect antibodies against SARS-CoV-2 in patient samples .
- Vaccine Development: The N protein is being explored as a potential antigen for vaccine formulations due to its conserved nature and ability to elicit a strong immune response .
- Research: Recombinant N protein is used in structural and functional studies to understand the mechanisms of viral replication and host interactions .
