Serine protease

Chymotrypsin (commonly referring to alpha-chymotrypsin) is a canonical pancreatic serine protease. Common laboratory preparations are typically purified from bovine or porcine pancreas and are frequently described commercially as “alpha-chymotrypsin from bovine pancreas” (CAS 9004-07-3). ...

Subtilisin-class proteases are a family of serine endoproteases predominantly secreted by bacteria, with Bacillus species as the most representative producers.

Endoproteinase Lys-C (Lys-C) is a lysine-specific serine endopeptidase that preferentially cleaves peptide bonds on the C-terminal side of lysine residues (Lys, K) under mildly alkaline conditions (typically pH 7.0–9.0).

Thrombin is a central serine protease in the coagulation cascade. It not only drives fibrin clot formation and promotes platelet activation, but—under specific cofactor conditions—also mediates anticoagulant pathways and cell signaling, thereby exhibiting marked pleiotropy in physiological ...

Serine proteases are widespread inside and outside cells and play key roles in proteolysis, signal transduction, and apoptosis. In protein extraction and purification, endogenous or exogenous serine proteases can rapidly cleave target proteins if left unchecked, severely compromising sample ...