SARS-CoV-2 S1 recombinant protein

Reference: PX-COV-P088-100
Product nameSARS-CoV-2 S1 recombinant protein
Expression systemEukaryotic expression
Molecular weight78.71 kDa
Purity estimated>90% by SDS-PAGE
BufferPBS pH 7.4, 1mM EDTA, 4% Trehalose, 1% Mannitol
FormLiquid
Delivery conditionDry Ice
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandProteoGenix
Host speciesMammalian cells
Fragment TypeSer13-Arg682, C-Terminal His Tag
Aliases /SynonymsS1 Protein, Spike glycoprotein, S glycoprotein, E2, Peplomer protein, S, SARS-CoV-2Spike protein S1
ReferencePX-COV-P088
NoteFor research use only. Not suitable for human use.

Description of SARS-CoV-2 S1 recombinant protein

Introduction

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of the ongoing COVID-19 pandemic. The virus is highly contagious and has resulted in millions of infections and deaths worldwide. One of the key components of the virus is the S1 protein, which plays a crucial role in viral entry into host cells. In recent years, there has been a growing interest in using SARS-CoV-2 S1 recombinant protein as a potential drug target, due to its structural and functional properties.

Structure of SARS-CoV-2 S1 Protein

The S1 protein is a glycoprotein that is located on the surface of the virus. It is composed of two subunits, S1 and S2, with the S1 subunit responsible for binding to host cell receptors. The S1 protein is further divided into two domains, the N-terminal domain (NTD) and the C-terminal domain (CTD). The NTD is responsible for binding to the host cell receptor, while the CTD is responsible for receptor recognition and membrane fusion. The S1 protein also contains a receptor-binding motif (RBM) within the CTD, which is crucial for binding to the angiotensin-converting enzyme 2 (ACE2) receptor on host cells.

Activity of SARS-CoV-2 S1 Protein

The S1 protein plays a critical role in viral entry into host cells. Upon binding to the ACE2 receptor, the S1 protein undergoes a conformational change, allowing the virus to fuse with the host cell membrane and release its genetic material into the cell. This process is essential for viral replication and the spread of infection. Additionally, the S1 protein is also involved in the evasion of the host immune response, making it an attractive target for drug development.

Application as a Drug Target

The S1 protein has been identified as a potential drug target due to its crucial role in viral entry and infection. Several studies have shown that targeting the S1 protein can inhibit viral entry and reduce the severity of infection. One approach is to use monoclonal antibodies that specifically bind to the RBM of the S1 protein, preventing its interaction with the ACE2 receptor. This strategy has shown promising results in preclinical studies and is currently being evaluated in clinical trials. Another approach is to develop small molecule inhibitors that can bind to the S1 protein and disrupt its function, preventing viral entry into host cells.

Use as an Antigen for Vaccine Development

The S1 protein is also a potential candidate for vaccine development against SARS-CoV-2. The RBM of the S1 protein is highly conserved among different strains of the virus, making it an ideal target for inducing a protective immune response. Several vaccine candidates, including mRNA and viral vector-based vaccines, have been designed to target the S1 protein. These vaccines aim to elicit the production of neutralizing antibodies that can block viral entry and prevent infection.

Conclusion

The SARS-CoV-2 S1 recombinant protein is a key component of the virus and plays a crucial role in viral entry and infection. Its structural and functional properties make it an attractive drug target for the treatment and prevention of COVID-19. Further research and development of S1 protein-based therapeutics and vaccines could potentially lead to effective treatments and control of the ongoing pandemic.

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