SARS-CoV-2 Spike RBD (318-541) Recombinant Protein (8xHis-Tag) #48801
Supporting Data
MW (kDa) | 34, 68 (non-reduced); 36 (reduced) |
Product Information
Formulation
Expression Host: Human (HEK293 cells)
Supplied in PBS solution (pH 7.2).
Supplied in PBS solution (pH 7.2).
Storage
Stable at -80°C for 3 years after receipt. Avoid repeated freeze-thaw cycles.
Product Description
SARS-CoV-2 Spike RBD (318-541) Recombinant Protein (8xHis-Tag) is derived from a recombinant expression construct corresponding to the host receptor-binding domain (RBD) of the SARS-CoV-2 spike protein. The expressed protein contains an 8xHis-Tag at its carboxy terminus.
MW (kDa) | 34, 68 (non-reduced); 36 (reduced) |
Purity | 98%, determined by SDS-PAGE. |
Background
The cause of the COVID-19 pandemic is a novel and highly pathogenic coronavirus, termed SARS-CoV-2 (severe acute respiratory syndrome coronavirus-2). SARS-CoV-2 is a member of the Coronaviridae family of viruses (1). The genome of SARS-CoV-2 is similar to other coronaviruses, and is comprised of four key structural proteins: S, the spike protein, E, the envelope protein, M, the membrane protein, and N, the nucleocapsid protein (2). Coronavirus spike proteins are class I fusion proteins and harbor an ectodomain, a transmembrane domain, and an intracellular tail (3,4). The highly glycosylated ectodomain projects from the viral envelope surface and facilitates attachment and fusion with the host cell plasma membrane. The ectodomain can be further subdivided into host receptor-binding domain (RBD) (S1) and membrane-fusion (S2) subunits, which are produced upon proteolysis by host proteases at S1/S2 and S2’ sites. S1 and S2 subunits remain associated after cleavage and assemble into crown-like homotrimers (2,4). In humans, both SARS-CoV and SARS-CoV-2 spike proteins utilize the angiotensin-converting enzyme 2 (ACE2) protein as a receptor for cellular entry (5-7). Spike protein subunits represent a key antigenic feature of coronavirus virions, and therefore represent an important target of vaccines, novel therapeutic antibodies, and small-molecule inhibitors (8,9).
- Zhou, P. et al. (2020) Nature 579, 270-3.
- Tortorici, M.A. and Veesler, D. (2019) Adv Virus Res 105, 93-116.
- Li, F. et al. (2006) J Virol 80, 6794-800.
- Li, F. (2016) Annu Rev Virol 3, 237-61.
- Shang, J. et al. (2020) Nature 581, 221-4.
- Wrapp, D. et al. (2020) Science 367, 1260-3.
- Yan, R. et al. (2020) Science 367, 1444-8.
- Yuan, Y. et al. (2017) Nat Commun 8, 15092.
- Amanat, F. and Krammer, F. (2020) Immunity 52, 583-9.
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