SARS Spike (1-53, 90-115, 171-205)
Protein is >90% pure as determined SDS-PAGE.
Description
The E.coli derived recombinant protein contains the Spike (1-53, 90-115, 171-205 a.a.) protein immunodominant regions fused to 6xHis tag at C-terminal.
Product Specs
Purified by proprietary chromatographic technique.
Immunoreactive with sera of SARS-infected individuals.
Product Science Overview
The SARS-Associated Coronavirus (SARS-CoV) spike protein is a crucial component of the virus’s structure, playing a significant role in its ability to infect host cells. The recombinant form of this protein, specifically the segments spanning amino acids 1-53, 90-115, and 171-205, has been extensively studied for its potential applications in research and therapeutic development.
The spike (S) protein of SARS-CoV is a transmembrane glycoprotein that facilitates the virus’s entry into host cells. It is composed of two subunits, S1 and S2. The S1 subunit contains the receptor-binding domain (RBD), which is responsible for binding to the host cell receptor, angiotensin-converting enzyme 2 (ACE2). The S2 subunit mediates the fusion of the viral and host cell membranes, allowing the viral genome to enter the host cell .
The recombinant spike protein segments (1-53, 90-115, 171-205 a.a.) are produced in E. coli and are fused to a His-tag for purification purposes . These segments are chosen for their relevance in the protein’s structure and function, particularly in the context of antibody recognition and vaccine development.
- Vaccine Development: The spike protein is a primary target for vaccine development due to its critical role in viral entry. Recombinant forms of the spike protein are used to elicit an immune response in the host, providing protection against the virus.
- Diagnostic Tools: Recombinant spike proteins are used in serological assays to detect antibodies against SARS-CoV in patient samples. This is essential for diagnosing past infections and understanding the spread of the virus.
- Therapeutic Research: The spike protein is also a target for therapeutic interventions, such as monoclonal antibodies that can neutralize the virus by blocking its ability to bind to ACE2.
Studies have shown that the spike protein’s interaction with ACE2 is a key determinant of the virus’s infectivity and pathogenicity . Structural analyses have revealed that specific mutations in the spike protein can enhance its binding affinity to ACE2, potentially increasing the virus’s transmissibility . Understanding these interactions is crucial for developing effective vaccines and therapeutics.
