SARS MERS, Sf9
Sf9, Baculovirus cells.
Middle East respiratory syndrome coronavirus, Human betacoronavirus 2c EMC/2012, MERS-CoV, MERS, MERSCoV SP, Spike glycoprotein, S glycoprotein, S, Spike protein, E2, Peplomer protein
Greater than 85.0% as determined by SDS-PAGE.
Description
SARS MERS Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 1285 amino acids (18-1296aa) and having a molecular mass of 141.6kDa.
SARS MERS 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. This virus belongs to the coronavirus family, known for causing illnesses ranging from the common cold to severe respiratory syndromes like SARS (severe acute respiratory syndrome). These illnesses can be life-threatening with high mortality rates. MERS-CoV, a novel strain in this family, leads to serious pneumonia and acute respiratory distress, often with a high fatality rate. As of January 27th, 2015, the World Health Organization (WHO) has documented 956 human infections and 351 deaths linked to MERS-CoV. The number of infections caused by this new coronavirus strain is predicted to rise. Similar to other coronaviruses, a large surface spike glycoprotein is crucial to the virus's structure. Situated on the virion's surface, this protein facilitates binding and entry into the host cell. The spike protein is divided into two domains: S1 and S2. The S1 domain is responsible for cell targeting and interaction, while the S2 domain mediates membrane fusion. A receptor binding domain located within the C-terminal of the S1 domain is a key focus for vaccine research and serves as a target for diagnostic development.
Recombinant SARS MERS protein, expressed in Sf9 insect cells using a baculovirus system, is a single, glycosylated polypeptide chain. This protein consists of 1285 amino acids (spanning from positions 18 to 1296), resulting in a molecular weight of 141.6 kDa. A 6-amino acid His-tag is fused to the C-terminus of the SARS MERS protein to facilitate purification, which is achieved through proprietary chromatographic methods.
The provided SARS MERS solution has a concentration of 0.25 mg/ml. It is formulated in a solution containing 10% glycerol and Phosphate-Buffered Saline (PBS) with a pH of 7.4.
For optimal storage, keep the SARS MERS protein vial at 4°C if it will be fully used within 2 to 4 weeks. For extended storage, it is recommended to freeze the protein at -20°C. To further enhance stability during long-term storage, the addition of a carrier protein such as 0.1% HSA (human serum albumin) or BSA (bovine serum albumin) is advisable. It is important to avoid repeated cycles of freezing and thawing to maintain protein integrity.
The purity of this protein is greater than 85%, as determined by SDS-PAGE analysis.
Middle East respiratory syndrome coronavirus, Human betacoronavirus 2c EMC/2012, MERS-CoV, MERS, MERSCoV SP, Spike glycoprotein, S glycoprotein, S, Spike protein, E2, Peplomer protein
Sf9, Baculovirus cells.
YVDVGPDSVK SACIEVDIQQ TFFDKTWPRP IDVSKADGII YPQGRTYSNI TITYQGLFPY QGDHGDMYVY SAGHATGTTP QKLFVANYSQ DVKQFANGFV VRIGAAANST GTVIISPSTS ATIRKIYPAF MLGSSVGNFS DGKMGRFFNH TLVLLPDGCG TLLRAFYCIL EPRSGNHCPA GNSYTSFATY HTPATDCSDG NYNRNASLNS FKEYFNLRNC TFMYTYNITE DEILEWFGIT QTAQGVHLFS SRYVDLYGGN MFQFATLPVY DTIKYYSIIP HSIRSIQSDR KAWAAFYVYK LQPLTFLLDF SVDGYIRRAI DCGFNDLSQL HCSYESFDVE SGVYSVSSFE AKPSGSVVEQ AEGVECDFSP LLSGTPPQVY NFKRLVFTNC NYNLTKLLSL FSVNDFTCSQ ISPAAIASNC YSSLILDYFS YPLSMKSDLS VSSAGPISQF NYKQSFSNPT CLILATVPHN LTTITKPLKY SYINKCSRLL SDDRTEVPQL VNANQYSPCV SIVPSTVWED GDYYRKQLSP LEGGGWLVAS GSTVAMTEQL QMGFGITVQY GTDTNSVCPK LEFANDTKIA SQLGNCVEYS LYGVSGRGVF QNCTAVGVRQ QRFVYDAYQN LVGYYSDDGN YYCLRACVSV PVSVIYDKET KTHATLFGSV ACEHISSTMS QYSRSTRSML KRRDSTYGPL QTPVGCVLGL VNSSLFVEDC KLPLGQSLCA LPDTPSTLTP RSVRSVPGEM RLASIAFNHP IQVDQLNSSY FKLSIPTNFS FGVTQEYIQT TIQKVTVDCK QYVCNGFQKC EQLLREYGQF CSKINQALHG ANLRQDDSVR NLFASVKSSQ SSPIIPGFGG DFNLTLLEPV SISTGSRSAR SAIEDLLFDK VTIADPGYMQ GYDDCMQQGP ASARDLICAQ YVAGYKVLPP LMDVNMEAAY TSSLLGSIAG VGWTAGLSSF AAIPFAQSIF YRLNGVGITQ QVLSENQKLI ANKFNQALGA MQTGFTTTNE AFQKVQDAVN NNAQALSKLA SELSNTFGAI SASIGDIIQR LDVLEQDAQI DRLINGRLTT LNAFVAQQLV RSESAALSAQ LAKDKVNECV KAQSKRSGFC GQGTHIVSFV VNAPNGLYFM HVGYYPSNHI EVVSAYGLCD AANPTNCIAP VNGYFIKTNN TRIVDEWSYT GSSFYAPEPI TSLNTKYVAP QVTYQNISTN LPPPLLGNST GIDFQDELDE FFKNVSTSIP NFGSLTQINT TLLDLTYEML SLQQVVKALN ESYIDLKELG NYTYYNKWPH HHHHH
Product Science Overview
The emergence of severe acute respiratory syndrome coronavirus (SARS-CoV) and Middle East respiratory syndrome coronavirus (MERS-CoV) has highlighted the importance of understanding the mechanisms behind viral entry into host cells. Both viruses belong to the betacoronavirus genus and share similarities in their spike (S) proteins, which play a crucial role in mediating viral entry by binding to host cell receptors.
The spike protein is a large, trimeric glycoprotein that protrudes 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, while the S2 subunit facilitates membrane fusion, allowing the viral genome to enter the host cell.
Recombination is a common phenomenon among coronaviruses, leading to the exchange of genetic material between different viral strains. This process can result in the emergence of new viral variants with altered properties, including changes in receptor binding and host range. In the case of SARS-CoV and MERS-CoV, recombination events have been observed in the RBD of the spike protein, which can significantly impact the virus’s ability to infect host cells .
SARS-CoV primarily uses angiotensin-converting enzyme 2 (ACE2) as its entry receptor, while MERS-CoV utilizes dipeptidyl peptidase 4 (DPP4). However, some studies suggest that recombination events between these viruses could potentially lead to the emergence of new variants capable of using alternative receptors, thereby expanding their host range .
Understanding the recombination events and structural changes in the spike protein is crucial for the development of effective vaccines. Recombinant spike proteins, which are engineered to mimic the native structure of the viral spike, are being investigated as potential vaccine candidates. These recombinant proteins can elicit strong immune responses, providing protection against viral infection .
