Recombinant SARS-CoV-2 BA.1.1 Spike RBD His-tag Protein (Catalog # 11131-CV) binds Recombinant Human ACE-2 Fc Chimera (10544-ZN) in a functional ELISA.
2 μg/lane of Recombinant SARS-CoV-2 BA.1.1 Spike RBD His-tag Protein (Catalog # 11131-CV) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, ...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
26 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
34-38 kDa, under reducing conditions
Publications
Read Publication using 11131-CV in the following applications:
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). A receptor binding domain (RBD) in the C-terminus of the S1
subunit has been identified and the RBD of SARS-CoV-2 shares 73% amino acid
(aa) identity with the RBD of the SARS-CoV-1, but only 22% aa identity with the
RBD of MERS‑CoV (6, 7). The low aa sequence homology is consistent with the
finding that SARS and MERS‑CoV bind different cellular receptors (8). The RBD
of SARS‑CoV‑2 binds a metallopeptidase,
angiotensin-converting enzyme 2 (ACE-2), similar to SARS-CoV-1, but with much higher affinity and faster binding
kinetics (9). Before binding to the ACE-2 receptor, structural analysis of the
S1 trimer shows that only one of the three RBD domains is in the "up"
conformation. This is an unstable and transient state that passes between
trimeric subunits but is nevertheless an exposed state to be targeted for
neutralizing antibody therapy (10). 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 (11). 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 (12). Several emerging SARS-CoV-2 genomes have been identified including
the Omicron, or B.1.1.529, variant. Additionally, several subvariants of
Omicron have been discovered, including the BA.2 and BA.1.1. First
identified in November 2021 in South Africa, the Omicron variant quickly became
the predominant SARS-CoV-2 variant. The Omicron
BA.1.1 contains an additional Arg346Lys mutation compared to the original Omicron variant. The
majority of the Omicron mutations are involved in ACE-2 binding and Omicron binds ACE-2
with greater affinity, potentially explaining its increased transmissibility and
viral fitness (13, 14, 15). Several of the RBD mutations are also identified in facilitating immune
escape and reducing neutralization activity to several monoclonal antibodies (13). Additionally, a series of novel
mutations are present in the RBD which have unknown impacts on receptor binding
or antibody neutralization.
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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