HEK293 Cells.
Spike glycoprotein, S glycoprotein, Peplomer protein, E2 glycoprotein precursor, Severe acute repiratory Syndrome-related Coronavirus, SARS, SRAS-CoV, SARS-CoV1, E2.
Greater than 95.0% as determined by SDS-PAGE.
The recombinant SARS Spike containing a total of 220 amino acids (306-515) and having a calculated Mw of 24.8 kDa.
SARS Spike is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
The SARS Coronavirus possesses an envelope with three key structural proteins: membrane (M), envelope (E), and spike (S) proteins. The spike (S) glycoprotein plays a crucial role in viral infection by binding to a cellular receptor, facilitating membrane fusion, and enabling the virus to enter susceptible cells. This critical function makes the S-protein a primary target for neutralizing antibodies.
This recombinant SARS Spike protein consists of 220 amino acids (spanning positions 306 to 515) and has a molecular weight of 24.8 kDa. A 6 amino acid His-tag is fused to the C-terminus to facilitate purification, which is achieved using proprietary chromatographic methods.
The SARS Spike (306-515) solution is provided at a concentration of 0.5mg/ml and is formulated in Phosphate-Buffered Saline (pH 7.4) with 10% Glycerol.
For optimal storage, the product should be kept at 4°C if it will be used within 2-4 weeks. For longer-term storage, it is recommended to freeze the product at -20°C. To further enhance stability during long-term storage, consider adding a carrier protein (0.1% HSA or BSA). Repeated freezing and thawing should be avoided.
The purity of the SARS Spike protein is greater than 95.0%, as determined by SDS-PAGE analysis.
The biological activity of the SARS Spike protein is assessed by its binding affinity to Human ACE-2 in a functional ELISA (using CAT# enz-1159).
Spike glycoprotein, S glycoprotein, Peplomer protein, E2 glycoprotein precursor, Severe acute repiratory Syndrome-related Coronavirus, SARS, SRAS-CoV, SARS-CoV1, E2.
HEK293 Cells.
DGSMRVVPSG DVVRFPNITN LCPFGEVFNA TKFPSVYAWE RKKISNCVAD YSVLYNSTFF STFKCYGVSA TKLNDLCFSN VYADSFVVKG DDVRQIAPGQ TGVIADYNYK LPDDFMGCVL AWNTRNIDAT STGNYNYKYR YLRHGKLRPF ERDISNVPFS PDGKPCTPPA LNCYWPLNDY GFYTTTGIGY QPYRVVVLSF ELLNAPATVC GPKLHHHHHH
The spike protein is a trimeric glycoprotein composed of two subunits, S1 and S2. The S1 subunit contains the RBD, which is responsible for recognizing and binding to the host cell receptor, angiotensin-converting enzyme 2 (ACE2) in the case of SARS-CoV-2 . The binding of the RBD to ACE2 is the first step in viral entry, followed by the fusion of the viral and cellular membranes mediated by the S2 subunit.
The RBD (306-515 a.a.) is a highly conserved region among coronaviruses, making it a prime target for vaccine and therapeutic development . This domain is crucial for the virus’s ability to infect host cells and is the primary target for neutralizing antibodies generated by the immune system.
Recombinant RBD refers to the RBD produced through 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:
The study of the RBD is crucial for understanding the mechanisms of viral entry and immune evasion. Mutations in the RBD can significantly impact the virus’s transmissibility and resistance to neutralizing antibodies . For instance, the Omicron variant of SARS-CoV-2 has multiple mutations in the RBD, which reduce the efficacy of vaccines and therapeutic antibodies developed against earlier strains .
Research on recombinant RBD has led to significant advancements in the development of vaccines and therapeutics. For example, the use of recombinant RBD in vaccine formulations has shown promise in inducing broad-spectrum immunity against multiple coronavirus variants . Additionally, recombinant RBD-based diagnostics have been instrumental in tracking the spread of the virus and assessing population immunity .