HomeProductsCoronavirus Research Tools(SARS-CoV-2) Spike Protein (RBD; 331-524)

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CV-3041-1
High-Purity Recombinant
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SKU: CV-3041-1

(SARS-CoV-2) Spike Protein (RBD; 331-524)

$108.00

The spike (S) glycoprotein of coronaviruses mediates entry into receptor-expressing host cells and plays the most important role in viral attachment, fusion, and entry; therefore, it serves as an important target for monoclonal antibodies, entry inhibitors, and vaccines. The S protein has two domains S1 and S2, where S1 facilitates initial binding to the receptor and the S2 domain drives membrane fusion and eventual entry of the virus. Within the S1 protein, the highly conserved receptor-binding domain (RBD) expresses a high affinity for the Angiotensin converting enzyme 2 receptor (ACE2). Experiments have shown that the RBD fragment blocked S-protein mediated infections and suggests potential as a viral attachment or entry inhibitor against SARS-CoV-2.

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Categories: Coronavirus Research Tools, COVID-19/ Sars-Cov-2 Related Proteins

Specifications

Physical State: White lyophilized powder
Temperature Storage: -20°C
Temperature Shipping: Ambient
Source: Recombinant. Expressed in E. coli
Purity: >97% by Mass Spec.
Molecular Mass: Theoretical

Amino Acid Sequence

D A E F R H D S G Y E V H H Q K L V F F A E D V G S N K G A I I G L M V G G V V

Description & Background

The spike (S) glycoprotein of coronaviruses mediates entry into receptor-expressing host cells and plays the most important role in viral attachment, fusion, and entry; therefore, it serves as an important target for monoclonal antibodies, entry inhibitors, and vaccines. The S protein has two domains S1 and S2, where S1 facilitates initial binding to the receptor and the S2 domain drives membrane fusion and eventual entry of the virus. Within the S1 protein, the highly conserved receptor-binding domain (RBD) expresses a high affinity for the Angiotensin converting enzyme 2 receptor (ACE2). Experiments have shown that the RBD fragment blocked S-protein mediated infections and suggests potential as a viral attachment or entry inhibitor against SARS-CoV-2.