Serine Protease
Serine proteases are enzymes that cleave peptide bonds in proteins, in which serine serves as the nucleophilic amino acid at the (enzyme's) active site. They are found ubiquitously in both eukaryotes and prokaryotes. Serine proteases fall into two broad categories based on their structure: chymotrypsin-like (trypsin-like) or subtilisin-like. In humans, they are responsible for co-ordinating various physiological functions, including digestion, immune response, blood coagulation and reproduction. Serine proteases are characterised by a distinctive structure, consisting of two beta-barrel domains that converge at the catalytic active site. These enzymes can be further categorised based on their substrate specificity as either trypsin-like, chymotrypsin-like or elastase-like.
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Aprotinin is a small protein serine protease inhibitor, used to reduce perioperative blood loss and transfusion.
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Sivelestat sodium tetrahydrate是人源白细胞弹性蛋白酶（neutrophil elastase）竞争性抑制剂，IC50值为44nM。
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Nafamostat甲磺酸盐是广谱的丝氨酸蛋白酶抑制剂，血管舒缓素抑制剂，能抑制血液凝固，还是潜在的补体抑制剂。
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AEBSF是水溶性的，不可逆的丝氨酸蛋白酶抑制剂,抑制蛋白酶如胰凝乳蛋白酶，激肽释放酶，血纤维蛋白溶酶，凝血酶，胰蛋白酶。
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Leupeptin hemisulfate is a reversible inhibitor of trypsin-like and cysteine proteases such as calpain.
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