CoV-2 S1, Sf9
Sf9, Baculovirus Cells.
Protein is >85% pure as determined SDS-PAGE.
Description
The Sf9 derived recombinant protein contains the Coronavirus 2019 CoV-2 Spike Glycoprotein S1, Wuhan-Hu-1 strain, amino acids 1-674 fused to His tag at C-terminal.
Product Specs
The novel coronavirus (2019-nCoV), responsible for causing viral pneumonia in humans, was first identified in December 2019 at a fish market in Wuhan, Hubei province, China.
Genetic analysis reveals that 2019-nCoV shares 87% sequence identity with the SARS-CoV-2 virus found in bats in Zhoushan, eastern China, in 2018. Despite some structural variations, the receptor-binding domain (RBD) of 2019-nCoV closely resembles that of the 2018 SARS-CoV, suggesting a potential for binding to the human ACE2 receptor (angiotensin-converting enzyme 2).
While bats are considered the likely natural reservoir of 2019-nCoV, it is suspected that an intermediary animal host, potentially from the seafood market, played a role in its transmission to humans. Research indicates that the 2019-nCoV genome is a product of recombination within the spike glycoprotein, likely between a bat coronavirus and an unknown coronavirus.
This recombinant protein, expressed in Sf9 insect cells, consists of the Spike Glycoprotein S1 subunit (amino acids 1-674) from the Wuhan-Hu-1 strain of the 2019 Coronavirus (CoV-2). It also includes a C-terminal His tag for purification.
The CoV-2 S1 protein solution is provided in Dulbecco's Phosphate-Buffered Saline (DPBS).
The CoV-2 S1 Glycoprotein is shipped with ice packs to maintain its stability. Upon receipt, it should be stored at -20°C.
The purity of the protein is greater than 85% as determined by SDS-PAGE analysis.
Sf9, Baculovirus Cells.
Purified by Metal-Afinity chromatographic technique.
Product Science Overview
The Coronavirus 2019 Spike Glycoprotein-S1 (SARS-CoV-2 S1) is a crucial component of the virus responsible for the COVID-19 pandemic. This glycoprotein plays a significant role in the virus’s ability to infect host cells and is a primary target for vaccine development and therapeutic interventions. The recombinant form of this protein, produced using the Sf9 insect cell-expression system, has been instrumental in research and vaccine development efforts.
The spike glycoprotein (S) of SARS-CoV-2 is a trimeric protein 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 angiotensin-converting enzyme 2 (ACE2) receptor on host cells. This binding is the first step in viral entry, leading to the fusion of the viral and cellular membranes facilitated by the S2 subunit .
The recombinant SARS-CoV-2 S1 protein is produced using the baculovirus expression system in Spodoptera frugiperda (Sf9) insect cells. This system is widely used for producing recombinant proteins due to its ability to perform post-translational modifications similar to those in mammalian cells. The recombinant S1 protein includes specific mutations to enhance its stability and expression .
The recombinant S1 protein has been pivotal in various research applications, including:
- Vaccine Development: It serves as an antigen in subunit vaccines, eliciting an immune response without the need for live virus. Novavax, for example, has developed a vaccine using a recombinant nanoparticle form of the full-length spike protein .
- Diagnostic Tools: The S1 protein is used in serological assays to detect antibodies against SARS-CoV-2 in individuals, helping to determine past infection or immune response to vaccination.
- Therapeutic Research: Studies have explored the interaction of the S1 protein with host cell receptors and its role in immune evasion, providing insights into potential therapeutic targets .
