SARS-CoV-2 Spike Glycoprotein Receptor Binding Domain L452R, T478K variant (rabbit IgG1 Fc-tagged)

Delta Variant|SARS-CoV-2 Spike RBD|SARS-CoV-2 Spike Receptor Binding Domain|Severe Acute Respiratory Syndrome Coronavirus 2 Spike Glycoprotein Receptor Binding Domain|Spike S1 RBD

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is an enveloped positive-stranded RNA virus, a member of the Betacoronavirus genus, and the causative agent of COVID-19.{53462,53459,53461,55257,55258} The SARS-CoV-2 spike glycoprotein, also known as the surface glycoprotein, is located on the outer envelope of the virion.{53462} It is composed of an S1 and S2 subunit divided by a furin S-cleavage site not found in other SARS-CoVs.{46767,49561} The S1 subunit contains the receptor-binding domain (RBD), which binds to the carboxypeptidase angiotensin-converting enzyme 2 (ACE2), and the S1 and S2 subunits are cleaved by the protease TMPRSS2 to facilitate viral fusion with the host cell membrane.{49542,49536,49558} In this way, ACE2 acts as the functional receptor for SARS-CoV-2. The SARS-CoV-2 variant of concern (VOC) B.1.617.2, also known as the delta variant, that was originally identified in India, contains the L452R and T478K substitutions.{65035} The leucine-to-arginine substitution at position 452 (L452R) increases SARS-CoV-2 affinity for human ACE2, decreases serum neutralization and binding with monoclonal antibodies, and promotes viral infectivity and replication.{65033,60562} The threonine-to-lysine substitution at position 478 (T478K) also induces structural changes in the receptor- and antibody-binding interfaces.{65034} Cayman's SARS-CoV-2 Spike Glycoprotein Receptor Binding Domain L452R, T478K variant (rabbit IgG1 Fc-tagged) protein can be used for ELISA and surface plasmon resonance (SPR) applications.

HEK293 cells

-80

-80

PBS, pH 7.4, with 5% mannitol, 5% D-(+)-trehalose, 0.01% Tween 20, and 10% glycerol

365

≥90% estimated by SDS-PAGE