SARS-CoV RBD recombinant protein (Arg306-Gln523)

Reference: PX-COV-P086-100
Product nameSARS-CoV RBD recombinant protein (Arg306-Gln523)
Expression systemEukaryotic expression
Molecular weight27.45 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 TypeArg306-Gln523
Aliases /SynonymsS glycoprotein, E2, Peplomer protein, Spike protein S1, Spike protein S2, Spike protein S2', S, 2, RBD, Receptor-Binding DomainSpike glycoprotein
ReferencePX-COV-P086
NoteFor research use only. Not suitable for human use.

Description of SARS-CoV RBD recombinant protein (Arg306-Gln523)

The Structure of SARS-CoV RBD Recombinant Protein

The SARS-CoV RBD (spike receptor-binding domain) recombinant protein is a key component of the SARS-CoV (severe acute respiratory syndrome coronavirus) virus. It is a protein that is responsible for binding to the host cell receptor and facilitating viral entry into the cell. The protein is made up of 193 amino acids and has a molecular weight of approximately 22 kDa.

The structure of the SARS-CoV RBD recombinant protein is complex and consists of multiple domains. The main domain, known as the receptor-binding motif (RBM), is responsible for binding to the host cell receptor, angiotensin-converting enzyme 2 (ACE2). This domain is made up of 193 amino acids and is highly conserved among different strains of the SARS-CoV virus.

In addition to the RBM, the SARS-CoV RBD recombinant protein also contains other domains such as the core domain, the fusion peptide, and the heptad repeat domains. These domains play important roles in the fusion of the virus with the host cell membrane and the subsequent release of the viral genome into the host cell.

The Activity of SARS-CoV RBD Recombinant Protein

The main activity of the SARS-CoV RBD recombinant protein is its ability to bind to the host cell receptor, ACE2. This binding is essential for the virus to enter the host cell and initiate infection. The RBM domain of the protein has a high affinity for ACE2, allowing for strong and specific binding.

In addition to its role in viral entry, the SARS-CoV RBD recombinant protein has also been found to induce the production of neutralizing antibodies in the host. These antibodies can block the binding of the virus to the host cell receptor, thus preventing infection. This makes the protein a potential target for the development of vaccines and therapeutics against SARS-CoV.

The Application of SARS-CoV RBD Recombinant Protein

The SARS-CoV RBD recombinant protein has several potential applications in the field of drug development and research. Its role as a key component of the SARS-CoV virus makes it a promising drug target for the development of antiviral drugs. By targeting the RBM domain, researchers can potentially block the virus from binding to the host cell and prevent infection.

In addition, the SARS-CoV RBD recombinant protein can also be used as an antigen in the development of vaccines against SARS-CoV. By introducing the protein into the body, the immune system can be stimulated to produce neutralizing antibodies that can protect against future infections.

Furthermore, the protein can also be used in diagnostic tests for SARS-CoV. By detecting the presence of the protein in a patient’s sample, healthcare professionals can confirm the diagnosis of SARS-CoV infection.

Conclusion

In summary, the SARS-CoV RBD recombinant protein is a key component of the SARS-CoV virus and plays a crucial role in viral entry and infection. Its complex structure and activity make it a potential drug target for the development of antiviral drugs and a promising antigen for the development of vaccines against SARS-CoV. With ongoing research and advancements in technology, the potential applications of this protein in the fight against SARS-CoV are constantly expanding.

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