HEK293
Lyophilized freezed dried powder.
Protein is >90% pure as determined SDS-PAGE.
The HEK293 derived recombinant protein contains the SARS Coronavirus spike S glycoprotein Receptor Binding Domain, amino acids 306-527 fused to His tag at C-terminal.
HEK293
Purified by immobilized metal affinity chromatographic technique.
The Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) is a member of the coronavirus family, which includes viruses that cause illnesses ranging from the common cold to more severe diseases such as Middle East Respiratory Syndrome (MERS) and COVID-19. The spike (S) protein of SARS-CoV plays a crucial role in the virus’s ability to infect host cells. The receptor-binding domain (RBD) within the spike protein is particularly important as it mediates the interaction between the virus and the host cell receptor, angiotensin-converting enzyme 2 (ACE2).
The spike protein of SARS-CoV is a transmembrane glycoprotein that forms homotrimers protruding from the viral surface. 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 ACE2. The RBD spans amino acids 306 to 527 in the spike protein sequence. This domain is critical for the virus’s ability to attach to and enter host cells.
The RBD of the spike protein undergoes conformational changes that facilitate the binding to ACE2. Upon binding, the spike protein is cleaved by host proteases, leading to the fusion of the viral and host cell membranes, allowing the viral genome to enter the host cell.
Recombinant RBD refers to the RBD that has been produced using recombinant DNA technology. This involves inserting the gene encoding the RBD into an expression system, such as bacteria, yeast, or mammalian cells, to produce the protein in large quantities. Recombinant RBD is used in various applications, including vaccine development, diagnostic assays, and therapeutic research.