Recombinant SARS-CoV-2 B.1.617.1 S GCN4-IZ Avi Protein, CF

Recombinant SARS-CoV-2 B.1.617.1 S GCN4-IZ Avi Protein, CF Summary

Product Specifications

Product Datasheets

Carrier Free

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Background: Spike

SARS-CoV-2, which causes the global pandemic coronavirus disease 2019 (Covid-19), belongs to a family of viruses known as coronaviruses that also include MERS-CoV and SARS-CoV-1. Coronaviruses are commonly comprised of four structural proteins: Spike protein (S), Envelope protein (E), Membrane protein (M) and Nucleocapsid protein (N) (1). The SARS-CoV-2 S protein is a glycoprotein that mediates membrane fusion and viral entry. The S protein is homotrimeric, with each ~180-kDa monomer consisting of two subunits, S1 and S2 (2). In SARS-CoV-2, as with most coronaviruses, proteolytic cleavage of the S protein into S1 and S2 subunits is required for activation. The S1 subunit is focused on attachment of the protein to the host receptor while the S2 subunit is involved with cell fusion (3-5). The S protein of SARS-CoV-2 shares 75% and 29% aa sequence identity with S protein of SARS-CoV-1 and MERS, respectively. The S Protein of the SARS-CoV-2 virus, like the SARS-CoV-1 counterpart, binds a metallopeptidase, Angiotensin-Converting Enzyme 2 (ACE-2), but with much higher affinity and faster binding kinetics through the receptor binding domain (RBD) located in the C-terminal region of S1 subunit (6). It has been demonstrated that the S Protein can invade host cells through the CD147/EMMPRIN receptor and mediate membrane fusion (7, 8). Polyclonal antibodies to the RBD of the SARS-CoV-2 protein have been shown to inhibit interaction with the ACE-2 receptor, confirming RBD as an attractive target for vaccinations or antiviral therapy (9). There is also promising work showing that the RBD may be used to detect presence of neutralizing antibodies present in a patient's bloodstream, consistent with developed immunity after exposure to the SARS-CoV-2 (10). Several emerging SARS-CoV-2 genomes have been identified with mutations compared to the Wuhan-Hu-1 SARS-CoV-2 reference sequence. Several emerging SARS-CoV-2 genomes have been identified with mutations in the RBD compared to the Wuhan-Hu-1 SARS-CoV-2 reference sequence. First detected in India in December 2020, the B.1.617.1, or Kappa, variant is considered a Variant of Interest (VOI) as it contains several mutations that potentially affect viral fitness and transmissibility. Both the L452R and E484Q mutations are found in the RBD and have been associated with resistance to neutralization by multiple monoclonal antibodies (11, 12). Further, the L452R/E484Q double mutation has been shown to have ~5-fold increased affinity for ACE-2 (12). The D614G mutation is located nearby to the RBD domain and has been shown to increase viral infectivity (13). The P618H mutation is found adjacent to the furin cleavage site and is proposed to enhance S protein cleavage and increase viral infectivity (14). Additionally, the E484K substitution alone has been shown to confer resistance to several monoclonal antibodies and is responsible for the first confirmed SARS-CoV-2 reinfection (15). Our Avi-tag Biotinylated SARS-CoV-2 Spike B.1.617.1 features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.

Related Research Areas

• Infectious Diseases