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SARS-CoV-2 B.1.1.529 (Omicron BA.1) RBD Alexa Fluor® 532-conjugated Antibody

R&D Systems, part of Bio-Techne | Catalog # FAB11227X

R&D Systems, part of Bio-Techne

Key Product Details

Species Reactivity

SARS-CoV-2

Applications

Blockade of Receptor-ligand Interaction, Immunocytochemistry

Label

Alexa Fluor 532 (Excitation = 534 nm, Emission = 553 nm)

Antibody Source

Monoclonal Mouse IgG1 Clone # 1056608

Product Specifications

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.

Clonality

Monoclonal

Host

Mouse

Isotype

IgG1

Applications

Application
Recommended Usage

Blockade of Receptor-ligand Interaction

Optimal dilution of this antibody should be experimentally determined.

Immunocytochemistry

Optimal dilution of this antibody should be experimentally determined.

Formulation, Preparation, and Storage

Purification

Protein A or G purified

Formulation

Supplied 0.2mg/ml in 1X PBS with RDF1 and 0.09% Sodium Azide

Shipping

The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.

Stability & Storage

Protect from light. Do not freeze. 12 months from date of receipt, 2 to 8 °C as supplied

Background: Spike RBD

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.

Long Name

Spike Receptor Binding Domain

Entrez Gene IDs

3200426 (HCoV-HKU1); 14254594 (MERS-CoV); 1489668 (SARS-CoV); 43740568 (SARS-CoV-2)

Gene Symbol

S

UniProt

Additional Spike RBD Products

Product Documents

Certificate of Analysis

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Note: Certificate of Analysis not available for kit components.

Product Specific Notices


This product is provided under an agreement between Life Technologies Corporation and R&D Systems, Inc, and the manufacture, use, sale or import of this product is subject to one or more US patents and corresponding non-US equivalents, owned by Life Technologies Corporation and its affiliates. The purchase of this product conveys to the buyer the non-transferable right to use the purchased amount of the product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The sale of this product is expressly conditioned on the buyer not using the product or its components (1) in manufacturing; (2) to provide a service, information, or data to an unaffiliated third party for payment; (3) for therapeutic, diagnostic or prophylactic purposes; (4) to resell, sell, or otherwise transfer this product or its components to any third party, or for any other commercial purpose. Life Technologies Corporation will not assert a claim against the buyer of the infringement of the above patents based on the manufacture, use or sale of a commercial product developed in research by the buyer in which this product or its components was employed, provided that neither this product nor any of its components was used in the manufacture of such product. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, Cell Analysis Business Unit, Business Development, 29851 Willow Creek Road, Eugene, OR 97402, Tel: (541) 465-8300. Fax: (541) 335-0354.

For research use only

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