Recombinant SARS-CoV-2 BA.2 Spike (GCN4-IZ) His-tag Protein (Catalog # 11109-CV) binds Recombinant Human ACE-2 Fc Chimera (10544-ZN) in a functional ELISA.
2 μg/lane of Recombinant SARS-CoV-2 BA.2 Spike (GCN4-IZ) His-tag Protein (Catalog # 11109-CV) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue ...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
144-172 kDa, under reducing conditions.
Publications
Read Publication using 11109-CV in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant SARS-CoV-2 BA.2 Spike (GCN4-IZ) His Protein, CF
2019-nCoV S Protein
2019-nCoV Spike
COVID-19 Spike
E2
Human coronavirus spike glycoprotein
Peplomer protein
S glycoprotein
S Protein
SARS-COV-2 S protein
SARS-COV-2 Spike glycoprotein
SARSCOV2 Spike protein
SARS-CoV-2
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% 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 including the Omicron, or B.1.1.529, variant. First identified in
November 2021 in South Africa, the Omicron variant quickly became the
predominant SARS-CoV-2 variant and is considered a variant of concern (VOC).
The Omicron variant contains 32 mutations in the S protein, 3 to 4 times more
than in other SARS-CoV-2 variants, that potentially affect viral fitness and transmissibility
(11). Of these mutations,15 are located in the RBD domain and allow the Omicron
variant to bind ACE-2 with greater affinity and, potentially, increased transmissibility
(11, 12). Several additional mutations throughout the S protein have been shown
or are predicted to enhance spike cleavage and could aid transmission (13-15).
The study of the Omicron variant's impact on immune escape and reduced
neutralization activity to monoclonal antibodies along with an increased risk
of reinfection, even among vaccinated individuals, remains ongoing (16). The BA.2 subvariant is predicted to be up to about 35 percent more transmissible than the original Omicron variant..
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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