Protease catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Protease is a serine endoproteinase with a broad specificity towards native and denatured proteins, and is active under alkaline conditions. It is active in some organic solvents such as dry octane.
The product has been used with other enzymes for in situ proteolysis to produce crystals suitable for structure determination. It has also been used in the process of isolation of subsarcolemmal (SS) and intermyofibrillar (IMF) mitochondria that can be used for functional in vitro studies. This is a proteolytic enzyme isolated from the fermentation of Bacillus licheniformis. It is a serine endoproteinase with a broad specificity towards native and denatured proteins, and is active under alkaline conditions.
