Description_x000D_ Specificity_x000D_ Subtilisin A is a member of the Serine S8 Endoproteinase family. It has broad specificity with a preference for a large uncharged residue in the P1 position. It hydrolyzes native and denatured proteins, and is active under alkaline conditions._x000D_ Application_x000D_ The enzyme from Sigma has been used to optimize release of all mitochondrial populations from homogenized ventricular tissue of rat heart. It has also been used in the pre-hybridisation treatment of formalin fixed, paraffin wax-embedded liver specimens for detecting human and viral DNA._x000D_ 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. Product P8038, also known as Subtilisin Carlsberg, has been used to hydrolyze cardiac cells to study the silencing of cardiac mitochondrial NHE1._x000D_ Packaging_x000D_ 1 g in glass bottle_x000D_ 50, 100, 250 mg in glass bottle_x000D_ Biochem/physiol Actions_x000D_ Proteinase catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate ._x000D_ Physical properties_x000D_ Subtilisin is a non-glycosylated single polypeptide chain without disulfide bonds and has a molecular weight of 27 KDa._x000D_ Unit Definition_x000D_ One unit will hydrolyze casein to produce color equivalent to 1.0 μmole (181 μg) of tyrosine per min at pH 7.5 at 37 °C (color by Folin-Ciocalteu reagent)._x000D_ Analysis Note_x000D_ Amino acid analysis and isoelectric focusing electrophoresis consistent with subtilisin Carlsberg.