Serine proteases are distributed among all living cells. The presences of nucleophilic Serine residue in the active site that attacks the carbonyl moiety of substrate, derives its name as serine protease. Ser proteases are endoproteases and catalyse polypeptide bond hydrolysis in the middle of the chain.
The human immune system consists of cells known as endosomal vesicles that are responsible for the expression of chymase and tryptase in mast cells, proteases in granulocytes and granzymes in lymphocytes. Serine proteases from endosomal vesicles are associated with inflammation, tissue remodelling, apoptosis and phagocytosis. An increase in serine protease activity contributes to pathology in allergy, autoimmune disorders and in cancer proliferation. Protease inhibitors specificity is very helpful in targeting some of the proteases which are known for pathogenesis in humans, viz. hepatitis, pancreatitis, cancer, arthritis, AIDS, emphysema, high blood pressure, thrombosis, muscular dystrophy. 
 Rachel, K. V., & Sirisha, G. V. D. (2017). Serine Proteases and Their Inhibitors in Human Health and Disease. Proteases in Human Diseases, 195–226. doi:10.1007/978-981-10-3162-5_10
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