HEK293 Cells.
Lyophilized freezed dried powder.
Protein is >95% pure as determined SDS-PAGE.
The HEK293 derived recombinant protein contains the Coronavirus 2019 Spike Glycoprotein S1 Receptor Binding Domain [ RBD ], Wuhan-Hu-1 strain, amino acids 319-541 fused to Fc tag at C-terminal.
The novel coronavirus responsible for the COVID-19 pandemic, initially named 2019-nCoV, was first identified in Wuhan, China, in December 2019. It likely originated from a seafood market. This virus is closely related to a bat coronavirus (SARS-CoV-2) discovered in 2018, sharing 87% of its genetic sequence. Both viruses utilize the ACE2 receptor (angiotensin-converting enzyme 2) in humans for cellular entry, though variations exist. While bats are considered the likely natural reservoir, an intermediary animal host, potentially from the seafood market, is suspected. Research indicates that the virus's spike glycoprotein may be a result of recombination between a bat coronavirus and another unknown coronavirus.
This product consists of the Receptor Binding Domain (RBD) of the SARS-CoV-2 Spike Glycoprotein S1, derived from the Wuhan-Hu-1 strain (amino acids 319-541). It is recombinantly produced in HEK293 cells and features a C-terminal Fc tag for purification and detection purposes.
The product is provided as a lyophilized powder, which means it has been freeze-dried to remove moisture for stability.
The lyophilized CoV-S1 RBD protein is formulated in a solution of 1x PBS (phosphate-buffered saline) at a pH of 7.4, with 5% trehalose added as a stabilizing agent.
The lyophilized CoV-2 S1 Glycoprotein RBD is stable at room temperature for up to three weeks. However, for long-term storage, it is recommended to store it desiccated (dry) at a temperature below -18°C. After reconstitution (adding liquid to the powder), the protein can be stored at 4°C for 2-7 days. For extended storage after reconstitution, store at -18°C. To ensure optimal stability during long-term storage, consider adding a carrier protein such as HSA or BSA at a concentration of 0.1%. Avoid repeated freeze-thaw cycles to maintain protein integrity.
The purity of the protein is greater than 95%, as determined by SDS-PAGE analysis, a widely used technique for separating and analyzing protein purity based on size.
HEK293 Cells.
Purified by Protein-G chromatographic technique.
The Coronavirus 2019 (COVID-19) pandemic, caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has led to significant global health challenges. One of the critical components of SARS-CoV-2 is the spike (S) glycoprotein, which plays a pivotal role in the virus’s ability to infect host cells. This article delves into the background of the Spike Glycoprotein-S1 Receptor Binding Domain (RBD) (319-541 a.a), Fc Recombinant, a crucial element in understanding and combating COVID-19.
The spike glycoprotein of SARS-CoV-2 is a type I membrane protein 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 angiotensin-converting enzyme 2 (ACE2) receptor on host cells . The specific region of interest, 319-541 amino acids (a.a), is within the S1 subunit and is critical for the virus’s attachment and entry into cells .
The RBD within the S1 subunit is a major target for neutralizing antibodies. These antibodies can block the interaction between the spike protein and the ACE2 receptor, thereby preventing the virus from entering host cells . This makes the RBD a focal point for vaccine development and therapeutic interventions.
The Fc recombinant fusion involves attaching the Fc region of an antibody to the RBD. This fusion enhances the stability and half-life of the RBD, making it more effective for use in vaccines and therapeutic applications . The Fc region also facilitates the recruitment of immune cells, enhancing the overall immune response against the virus.