Home > Signal Pathway > Proteases > Serine Protease

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.
  • Aprotinin EY2819

    Aprotinin is a small protein serine protease inhibitor, used to reduce perioperative blood loss and transfusion.

  • Sivelestat sodium EY2742

    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。

  • Nafamostat Mesylate EY1792


  • AEBSF HCl EY0983


  • Leupeptin Hemisulfate EY0795

    Leupeptin hemisulfate is a reversible inhibitor of trypsin-like and cysteine proteases such as calpain.

  • Current page1, Total Pages2, Total Record7 First Prev 12 Next Last Goto