SARS MERS S2
Sf9, Baculovirus cells.
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
Greater than 85.0% as determined by SDS-PAGE.
Description
SARS MERS S2 Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 554 amino acids (752-1296aa) and having a molecular mass of 60.7kDa.
SARS MERS S2 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Product Specs
The Middle East Respiratory Syndrome Coronavirus (MERS-CoV) has been a concern since April 2012, with cases reported globally. Coronaviruses, responsible for illnesses like the common cold and SARS, can be severe and even fatal. MERS-CoV, a novel coronavirus, causes serious respiratory problems and pneumonia, often leading to death. As of January 27th, 2015, the World Health Organization (WHO) has documented 956 human cases and 351 fatalities. The virus's spike glycoprotein, particularly the S1 domain, plays a crucial role in its ability to infect cells, making it a key target for vaccine research and diagnostic testing.
SARS MERS S2 Recombinant, expressed using Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain. It comprises 554 amino acids (752-1296aa), resulting in a molecular weight of 60.7kDa. The protein is engineered with a 6 amino acid His-tag at the C-terminus and undergoes a purification process using specialized chromatographic methods.
The SARS MERS S2 solution is provided at a concentration of 0.25mg/ml. The solution is formulated with 10% glycerol and Phosphate-Buffered Saline at a pH of 7.4.
For optimal storage and to maintain product integrity, adhere to the following guidelines: - If the entire vial is intended for use within 2-4 weeks, it should be stored at 4°C. - For prolonged storage, freezing at -20°C is recommended. - When storing for extended periods, adding a carrier protein (0.1% HSA or BSA) is advisable. - To preserve product quality, minimize exposure to repeated freeze-thaw cycles.
The purity of the SARS MERS S2 protein is determined to be greater than 85.0% using SDS-PAGE analysis.
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
Sf9, Baculovirus cells.
ADPSVPGEMR LASIAFNHPI QVDQLNSSYF KLSIPTNFSF GVTQEYIQTT IQKVTVDCKQ YVCNGFQKCE QLLREYGQFC SKINQALHGA NLRQDDSVRN LFASVKSSQS SPIIPGFGGD FNLTLLEPVS ISTGSRSARS AIEDLLFDKV TIADPGYMQG YDDCMQQGPA SARDLICAQY VAGYKVLPPL MDVNMEAAYT SSLLGSIAGV GWTAGLSSFA AIPFAQSIFY RLNGVGITQQ VLSENQKLIA NKFNQALGAM QTGFTTTNEA FQKVQDAVNN NAQALSKLAS ELSNTFGAIS ASIGDIIQRL DVLEQDAQID RLINGRLTTL NAFVAQQLVR SESAALSAQL AKDKVNECVK AQSKRSGFCG QGTHIVSFVV NAPNGLYFMH VGYYPSNHIE VVSAYGLCDA ANPTNCIAPV NGYFIKTNNT RIVDEWSYTG SSFYAPEPIT SLNTKYVAPQ VTYQNISTNL PPPLLGNSTG IDFQDELDEF FKNVSTSIPN FGSLTQINTT LLDLTYEMLS LQQVVKALNE SYIDLKELGN YTYYNKWPHH HHHH
Product Science Overview
The SARS-CoV-2 virus, responsible for the COVID-19 pandemic, and the MERS-CoV virus, responsible for the Middle East Respiratory Syndrome (MERS), are both members of the Coronaviridae family. These viruses have spike (S) glycoproteins on their surfaces, which play a crucial role in viral entry into host cells. The spike protein is divided into 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.
The S2 subunit of the spike protein is highly conserved across different coronaviruses, including SARS-CoV-2 and MERS-CoV. This conservation makes it an attractive target for vaccine and therapeutic development. The S2 subunit contains several important regions, including the fusion peptide, heptad repeat regions (HR1 and HR2), and the transmembrane domain. These regions are critical for the fusion process that allows the virus to enter host cells .
Recombinant S2 proteins are produced using genetic engineering techniques to express the S2 subunit in various host systems, such as bacteria, yeast, or mammalian cells. These recombinant proteins can be used in research to study the structure and function of the S2 subunit, as well as in the development of vaccines and therapeutics. The use of recombinant S2 proteins allows for the production of large quantities of the protein, which is essential for these applications .
- Broad Neutralization: The S2 subunit is more conserved than the S1 subunit, which means that antibodies targeting S2 may be effective against a wider range of coronavirus variants. This broad neutralization potential is particularly important given the rapid emergence of new variants .
- Cross-Reactivity: Antibodies targeting the S2 subunit may also cross-react with other coronaviruses, such as MERS-CoV and common cold coronaviruses. This cross-reactivity could provide broader protection against multiple coronaviruses .
- Memory B-Cell and T-Cell Responses: The S2 subunit has been shown to elicit strong memory B-cell and T-cell responses, which are important for long-term immunity. These responses can help provide lasting protection against infection .
Despite the potential benefits, there are several challenges associated with the development of S2-based vaccines and therapeutics:
- Glycan Shielding: The S2 subunit is heavily glycosylated, which can shield it from recognition by the immune system. Understanding the role of glycans in the accessibility and stability of the S2 subunit is crucial for the design of effective vaccines and therapeutics .
- Antigenic Variation: While the S2 subunit is more conserved than S1, it is not completely immune to mutations. Continued surveillance of emerging variants is necessary to ensure the effectiveness of S2-based interventions .
- Antibody-Dependent Enhancement (ADE): There is a risk that antibodies targeting the S2 subunit could enhance viral entry into host cells, a phenomenon known as ADE. Further research is needed to understand and mitigate this risk .
