SARS-CoV-2 Spike Glycoprotein S1 Subunit (recombinant)

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. The SARS-CoV-2 spike glycoprotein, also known as the surface glycoprotein, is located on the outer envelope of the virion. It is composed of an S1 and S2 subunit divided by a furin S-cleavage site not found in other SARS-CoVs. 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. The SARS-CoV-2 spike glycoprotein S1 subunit induces inflammatory gene expression in the frontal cortex, hippocampus, and hypothalamus, as well as activates toll-like receptor 2 (TLR2) and TLR4 signaling and increases social avoidance in the juvenile social exploration test in rats. Cayman's SARS-CoV-2 Spike Glycoprotein S1 Subunit (recombinant) can be used for ELISA. This protein is a disulfide-linked homodimer. The reduced monomer, composed of the SARS-CoV-2 spike glycoprotein S1 subunit (amino acids 16-685) fused to mouse IgG1 Fc at its C-terminus, consists of 904 amino acids and has a calculated molecular weight of 101.4 kDa. As a result of glycosylation, the monomer migrates at approximately 116 kDa by SDS-PAGE under reducing conditions.Synonyms: COVID-19 Surface Glycoprotein S1 Subunit, 2019-nCoV Surface Glycoprotein S1 Subunit, SARS-CoV-2 Surface Glycoprotein S1 Subunit, Severe Acute Respiratory Syndrome Coronavirus 2 Spike Glycoprotein S1 Subunit. Purity: >90% estimated by SDS-PAGE. Endotoxin Testing: <1.0 EU/µg, determined by the LAL endotoxin assay. Source: Active recombinant C-terminal mouse IgG1 Fc-tagged SARS-CoV-2 surface glycoprotein S1 subunit expressed in HEK293 cells. Amino Acids: 16-685. MW: 101.4 kDa. Formulation: (Request formulation change), Lyophilized from sterile PBS, pH 7.4. UniProt Accession #: P0DTC2.