Middle East respiratory syndrome coronavirus, Human betacoronavirus 2c EMC/2012, MERS-CoV, MERSCoV S2 P, Spike2 glycoprotein, S2 glycoprotein, S2, Spike S2 Subunit protein, S2 Subunit
Sterile filtered colorless solution
The Middle East Respiratory Syndrome Coronavirus (MERS-CoV) has been responsible for outbreaks since April 2012. Coronaviruses, such as those responsible for the common cold and SARS (severe acute respiratory syndrome), can cause severe illness and mortality. MERS-CoV is a novel coronavirus that causes severe pneumonia and respiratory illness. As of January 27th, 2015, the World Health Organization (WHO) has reported 956 human cases and 351 deaths. The virus's large surface spike glycoprotein is crucial for binding and entering target cells. This protein has two domains: S1, responsible for cellular tropism and target cell interaction, and S2, responsible for membrane fusion. The S1 domain's C-terminal contains a receptor binding domain, a potential target for vaccine development and diagnostic antigen.
A sterile, colorless solution.
The solution contains 1mg/ml of SARS MERS Spike S2 antibody in a Phosphate-Buffered Saline (pH 7.4) with 0.02% Sodium Azide and 10% Glycerol.
For short-term storage (up to 1 month), keep at 4°C. For long-term storage, store at -20°C. Avoid repeated freeze-thaw cycles.
The product is stable for 12 months at -20°C and 1 month at 4°C.
SARS MERS Spike S2 antibody has been validated for specificity and reactivity using ELISA and Western blot analysis. Optimal results may require titration based on the specific application.
Middle East respiratory syndrome coronavirus, Human betacoronavirus 2c EMC/2012, MERS-CoV, MERSCoV S2 P, Spike2 glycoprotein, S2 glycoprotein, S2, Spike S2 Subunit protein, S2 Subunit
SARS MERS Spike S2 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
PAT14H8AT
Recombinant MERS-CoV Spike S2 Subunit (752-1296aa) purified from Baculovirus.
IgG2b kappa
The spike (S) protein of coronaviruses, including SARS-CoV-2 (responsible for COVID-19), SARS-CoV (responsible for SARS), and MERS-CoV (responsible for MERS), plays a crucial role in the virus’s ability to infect host cells. The spike protein is composed of two subunits: S1 and S2. The S1 subunit is responsible for binding to the host cell receptor, while the S2 subunit facilitates the fusion of the viral and host cell membranes, enabling viral entry.
The S2 subunit is highly conserved across different coronaviruses, making it an attractive target for broad-spectrum antiviral strategies. Unlike the S1 subunit, which undergoes significant antigenic variation, the S2 subunit remains relatively stable. This stability makes the S2 subunit a prime target for the development of cross-reactive antibodies that can neutralize multiple coronavirus strains .
Mouse anti-SARS/MERS spike S2 antibodies are monoclonal antibodies generated in mice that specifically target the S2 subunit of the spike protein. These antibodies are valuable tools for research and therapeutic development for several reasons:
Recent studies have identified several mouse anti-S2 antibodies that exhibit broad neutralizing activity against multiple coronavirus strains. For example, one study reported the identification of an antibody that binds to a highly conserved epitope in the fusion peptide of the S2 subunit, demonstrating broad neutralization across SARS-CoV-2 variants, SARS-CoV, and related zoonotic sarbecoviruses .