Spike RBD Antibody (L009.1.32H) [Unconjugated] Summary
| Additional Information |
Recombinant Monoclonal Antibody. Bivalent Llama VHH domain, Human IgG2 Fusion Antibody. |
| Immunogen |
Human embryonic kidney cell HEK293-derived SARS-CoV-2 Spike RBD as immunogen for bivalent Llama VHH-Human IgG2 Fusion Antibody.
Arg319-Phe541
Accession # YP_009724390.1 |
| Specificity |
Clone L009.1.32H is a bivalent Llama V HH-Human IgG 2 Fusion Antibody that detects SARS-CoV-2 Spike RBD in direct ELISAs. Antibody construct is depicted below. SARS-CoV-2 Spike RBD Specific
Llama VHH domain | Llama Hinge | Human IgG2 | | N-terminus | | C-terminus | |
|
| Source |
N/A |
| Clonality |
Monoclonal |
| Host |
Llama |
| Purity Statement |
Protein A or G purified from cell culture supernatant |
| Endotoxin Note |
<0.10 EU per 1 μg of the antibody by the LAL method. |
| 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 50 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 (L009.1.32H) [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 are commonly comprised of four structural proteins: Spike
protein(S), Envelope protein (E), Membrane protein (M), and Nucleocapsid
protein (N) (1). SARS-CoV-2 Spike
Protein (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 two distinct peptides, 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). Based on structural biology studies, the receptor binding domain
(RBD), located in the C-terminal region of S1, can be oriented either in the
up/standing or down/lying state (6). The standing state is associated with
higher pathogenicity and both SARS-CoV-1 and MERS can access this state due to
the flexibility in their respective RBDs. A similar two-state structure and
flexibility is found in the SARS-CoV-2 RBD (7). Based on amino acid (aa)
sequence homology, the SARS-CoV-2 S1 subunit RBD has 73% identity with the RBD
of the SARS-CoV-1 S1 RBD, but only 22% homology with the MERS S1 RBD. The low aa sequence homology is consistent
with the finding that SARS and MERS bind different cellular receptors (8). The
S Protein of the SARS-CoV-2 virus, like the SARS-CoV-1 counterpart, binds
Angiotensin-Converting Enzyme 2 (ACE2), but with much higher affinity and
faster binding kinetics (9). Before binding to the ACE2 receptor, structural
analysis of the S1 trimer shows that only one of the three RBD domains in the
trimeric structure 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 ACE2 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 virus (12). Lastly, it has been demonstrated the S Protein
can invade host cells through the CD147/EMMPRIN receptor and mediate membrane fusion (13, 14).
- 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.
- Yuan, Y. et al. (2017) Nat. Commun. 8:15092.
- Walls, A.C. et al. (2010) Cell 180:281.
- 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. https://doi.org/10.1016/j.it.2020.03.007.
- Okba, N. M. A. et al. (2020). Emerg. Infect. Dis. https://doi.org/10.3201/eid2607.200841.
- Wang, X. et al. (2020) https://doi.org/10.1038/s41423-020-0424-9.
- Wang, K. et al. (2020) bioRxiv https://www.biorxiv.org/content/10.1101/2020.03.14.988345v1.
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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