Spike RBD Antibody (1056608) [Unconjugated] Summary
Immunogen |
Recombinant SARS-CoV-2 B.1.1.529 (Omicron) Spike RBD domain. Arg319-Phe541 Accession # YP_009724390.1 |
Specificity |
It detects SARS-CoV-2 Omicron BA.1 in Direct ELISA. In ELISA, this antibody does not detect SARS-CoV-2 Alpha, Gamma or Delta variants. |
Source |
N/A |
Isotype |
IgG1 |
Clonality |
Monoclonal |
Host |
Mouse |
Purity Statement |
Protein A or G purified from cell culture supernatant |
Innovator's Reward |
Test in a species/application not listed above to receive a full credit towards a future purchase. |
Applications/Dilutions
Dilutions |
- Blockade of Receptor-ligand Interaction
- Immunocytochemistry 3-25 ug/mL
|
Packaging, Storage & Formulations
Storage |
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.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS. |
Reconstitution Instructions |
Reconstitute at 0.5 mg/mL in sterile PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Spike RBD Antibody (1056608) [Unconjugated]
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). 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. 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 15 mutations
in RBD domain that potentially affect viral fitness and
transmissibility. The
majority of the mutations are involved in ACE-2 binding and Omicron
binds ACE-2
with greater affinity, potentially explaining its increased
transmissibility (13,
14). Several of these mutations are also identified in facilitating
immune
escape and reducing neutralization activity to several monoclonal
antibodies (13). Additionally, a series of new 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.
- Li, W. et al. (2003) Nature 426:450.
- Wong, S.K. et al. (2004) J. Biol. Chem. 279:3197.
- Jiang, S. et al. (2020) Trends. Immunol. https://doi.org/10.1016/j.it.2020.03.007.
- Ortega, J.T. et al. (2020) EXCLI J. 19:410.
- Wrapp, D. et al. (2020) Science 367:1260.
- Tai, W. et al. (2020) Cell. Mol. Immunol. 17:613.
- Okba, N.M.A. et al. (2020). Emerg. Infect. Dis. https://doi.org/10.3201/eid2607.200841.
- Shah, M. and H.G. Woo (2022) Front. Immunol. https://doi.org/10.3389/fimmu.2021.830527.
- Lupala, C.S. et al. (2021) Biochem. Biophys. Res. Comm. (2022) https://doi.org/10.1101/2021.12.10.472102.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are
guaranteed for 1 year from date of receipt.
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