CoV-2-S1 (319-541)
HEK293 Cells.
Protein is >90% pure as determined SDS-PAGE.
Description
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 His tag at C-terminal.
Product Specs
In December 2019, a novel coronavirus, designated as 2019-nCoV, emerged in Wuhan, China, causing viral pneumonia in humans. The virus was linked to a seafood market in the city.
Genetic analysis revealed that 2019-nCoV shares a high degree of similarity (87%) with bat-derived SARS-CoV-2, specifically a strain identified in Zhoushan, eastern China. Notably, the receptor-binding domain (RBD) structure of 2019-nCoV closely resembles that of 2018 SARS-CoV, suggesting a potential for binding to the human ACE2 receptor, despite some amino acid variations.
While bats are considered the likely reservoir of 2019-nCoV, the presence of other animal species at the seafood market raised suspicions of an intermediate host. Research indicates that the virus's spike glycoprotein might be a product of recombination between a bat coronavirus and an unknown coronavirus.
This recombinant protein is derived from HEK293 cells and encompasses the Receptor Binding Domain (RBD) of the SARS-CoV-2 Spike Glycoprotein S1, specifically the Wuhan-Hu-1 strain (amino acids 319-541). It is expressed with a C-terminal His tag for purification and detection purposes.
This product consists of CoV-S1 RBD protein at a concentration of 1mg/ml in a buffer composed of 20mM sodium phosphate (NaPP), 300mM NaCl, at pH 7.2.
CoV-2 S1 RBD Protein is shipped with ice packs to maintain its stability. Upon receiving the product, it is recommended to store it at -20°C to preserve its integrity.
The biological activity of SARS CoV-2 Spike Glycoprotein S1 RBD was validated through its interaction with recombinant ACE2 receptor protein. This binding affinity was confirmed using a structural complementation reporter assay known as NanoBiT®.
The purity of this protein is greater than 90%, as determined by SDS-PAGE analysis.
HEK293 Cells.
Purified by Metal-Afinity chromatographic technique.
Product Science Overview
The Coronavirus 2019 (COVID-19) pandemic, caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has led to extensive research on its structural proteins, particularly the spike (S) glycoprotein. The spike glycoprotein is crucial for the virus’s ability to infect host cells. This article delves into the background of the recombinant form of the spike glycoprotein’s S1 receptor-binding domain (RBD), specifically the amino acid sequence from 319 to 541.
The spike glycoprotein of SARS-CoV-2 is a trimeric class I fusion protein that facilitates viral 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 host cell receptor, angiotensin-converting enzyme 2 (ACE2). The S2 subunit mediates the fusion of the viral and cellular membranes.
The RBD within the S1 subunit spans amino acids 319 to 541. This domain is critical for the virus’s ability to attach to ACE2, initiating the process of viral entry. The binding affinity of the RBD to ACE2 is a key determinant of the virus’s infectivity and transmissibility .
Recombinant forms of the RBD are produced using various expression systems, such as mammalian cells, insect cells, and yeast. These recombinant proteins are used in research to study the virus’s interaction with host cells, develop vaccines, and screen for potential therapeutic agents.
The recombinant RBD retains the ability to bind ACE2, making it a valuable tool for understanding the molecular mechanisms of SARS-CoV-2 infection. It is also used in serological assays to detect antibodies against SARS-CoV-2 in patient samples .
Glycosylation, the addition of carbohydrate groups to the spike protein, plays a significant role in the virus’s ability to evade the host immune system. The RBD contains several glycosylation sites that can affect its structure and function. For example, the presence of a glycan at position N343 within the RBD has been shown to modulate the virus’s sensitivity to neutralizing antibodies .
The RBD is a major target for neutralizing antibodies, making it a critical component in vaccine design. Vaccines that elicit a strong immune response against the RBD can potentially block the virus’s ability to bind to ACE2 and prevent infection. Several COVID-19 vaccines, including mRNA-based vaccines, incorporate the RBD or the full-length spike protein to induce protective immunity .
