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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 NOWViral main protease (Mpro), also known as 3C-like protease (3CLpro), is a viral protease that mediates the replication and transcription of severe acute respiratory syndrome coronavirus (SARS-CoV) and SARS-CoV-2, the causative agents of SARS and COVID-19, respectively.1,2 Mpro digests SARS-CoV and SARS-CoV-2 viral polyproteins at 11 conserved sites, beginning with autolytic cleavage of itself, to release the functional peptides required for viral replication and transcription. Covidyte™ EN450 is a fluorogenic substrate for Mpro that contains 14 amino acids, KTSAVLQSGFRKME, which are recognized by Mpro. Upon enzymatic cleavage by Mpro, EDANS is separated from the Dabcyl quencher, displays excitation/emission maxima of 350/460 nm, respectively, and can be used to quantify Mpro activity.
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1. Characterization of SARS main protease and inhibitor assay using a fluorogenic substrate. Biochem. Biophys. Res. Commun. 318(4), 862-867 (2004).
2. Discovery of M protease inhibitors encoded by SARS-