Recombinant SARS-CoV-2 P.1 Spike (GCN4-IZ) His-tag (Catalog # 10795-CV) binds Recombinant Human ACE-2 His-tag (933-ZN) in a functional ELISA.
2 μg/lane of Recombinant SARS-CoV-2 P.1 Spike GCN4-IZ His-tag (Catalog # 10795-CV) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing ...read more
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
138 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
140-170 kDa, under reducing conditions.
Publications
Read Publications using 10795-CV in the following applications:
Severe Acute Respiratory Syndrome Coronavirus 2 Spike Protein
Spike glycoprotein
Spike
surface glycoprotein
Background
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% amino acid 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 including the P.1 (Brazilian) variant (11). The P.1 variant contains
3 mutations of interest in the RBD domain: K417T, E484K, and N501Y (11). 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 (12). Structural analysis points to E484K as a potentially crucial
mutation as it creates a new site for hACE-2 binding and may enhance binding
affinity (13).
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.
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