Recombinant SARS-CoV-2 B.1.617.2 S GCN4-IZ Avi Protein, CF
Recombinant SARS-CoV-2 B.1.617.2 S GCN4-IZ Avi Protein, CF Summary
Learn more about Avi-tag Biotinylated ProteinsProduct Specifications
| SARS-CoV-2 B.1.617.2 Spike (Val16-Lys1211)(Thr19Arg, Gly142Asp, Glu156Gly, Phe157 del, Arg158 del, Leu452Arg, Thr478Lys, Asp614Gly, Pro681Arg, Asp950Asn)(Arg682Ser, Arg685Ser, Lys986Pro, Val987Pro) Accession # YP_009724390.1 | GCN4-IZ | Avi-tag | 6-His tag |
| N-terminus | C-terminus | ||
Analysis
Product Datasheets
AVI10878
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.
AVI10878
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
| Reconstitution | Reconstitute at 500 μg/mL in PBS. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Scientific Data
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Biotinylated Recombinant SARS-CoV-2 B.1.617.2 Spike (GCN4-IZ) Avi-tag His-tag (Catalog # AVI10878) binds Recombinant Human ACE-2 Fc Chimera (10544-ZN) in a functional ELISA.
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2 μg/lane of Biotinylated Recombinant SARS-CoV-2 B.1.617.2 S (GCN4-IZ) Avi-tag His-tag Protein (Catalog # AVI10878) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR)conditions and visualized by Coomassie® Blue staining, showing bands at 144-170 kDa.
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 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). A metallopeptidase, angiotensin-converting enzyme 2 (ACE-2), has been identified as a functional receptor for SARS-CoV-2 through interaction with a receptor binding domain (RBD) located at the C-terminus of S1 subunit (6, 7). The S protein of SARS-CoV-2 shares 75% and 29% amino acid sequence identity with S protein of SARS-CoV-1 and MERS, respectively. The SARS-CoV-2 delta variant (B.1.617.2) carrying the amino acid substitution L452R and T478K in the RBD was identified as a prevalent strain in India and has been detected in more than 40 countries (8, 9). It has higher transmissible rate and more resistant to vaccine (10). Our Avi-tag Biotinylated SARS-CoV-2 B.1.617.2 Spike (GCN4-IZ) His-tag 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.
- Wu, F. et al. (2020) Nature 579:265.
- Tortorici, M.A. and D. Veesler (2019) Adv. Virus Res. 105:93.
- Bosch, B.J. et al. (2003). J. Virol. 77:8801.
- Belouzard, S. et al. (2009) Proc. Natl. Acad. Sci. 106:5871.
- Millet, J.K. and G.R. Whittaker (2015) Virus Res. 202:120.
- Li, W. et al. (2003) Nature 426:450.
- Wong, S.K. et al. (2004) J. Biol. Chem. 279:3197.
- Yadav, P.D. et al. (2021) bioRxiv https://doi.org/10.1101/2021.04.23.441101.
- Cherian, S. et al. (2021) bioRxiv https://doi.org/10.1101/2021.04.22.440932.
- Bernal, J. et al. (2021) medRxiv https://doi.org/10.1101/2021.05.22.21257658.
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