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Item No. 31815

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Explore how neutrophils shape the immune response in health and disease. This poster highlights neutrophil pathogen defense mechanisms, including phagocytosis, degranulation, and NETosis, as well as neutrophil roles in inflammation and NET-associated pathologies.
DOWNLOAD NOWSevere 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-19.1,2,3,4,5 The SARS-CoV-2 spike glycoprotein, also known as the surface glycoprotein, is a viral structural protein encoded by the S gene in SARS-CoV-2 RNA.1 It is composed of an S1 and S2 subunit divided by a furin S-cleavage site not found in other SARS-CoVs.6,7 The C-terminal S2 subunit, which facilitates fusion between viral and host cell membranes, contains a fusion peptide (FP) and two heptad repeats (HRs), as well as transmembrane and cytoplasmic domains.7,8 Upon insertion of the FP in the target cell membrane, the HRs form a six-helical bundle (6-HB) that enables SARS-CoV-2 to fuse with the target cell. The SARS-CoV-2 spike glycoprotein S2 subunit increases amyloid-β (1-40) (Aβ40) and Aβ42 levels in primary mouse neuron culture supernatants and the number of hippocampal and cortical Aβ plaques in APPswe/PSEN1dE9 transgenic mice.9 Cayman's SARS-CoV-2 Spike Glycoprotein S2 Subunit (recombinant) protein is a disulfide-linked homodimer. The reduced monomer, composed of the SARS-CoV-2 spike glycoprotein S2 subunit (amino acids 686-1,213) fused to mouse IgG1 Fc at its C-terminus, consists of 762 amino acids and has a calculated molecular weight of 84.3 kDa.
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