Description_x000D_ Specificity_x000D_ A mixture of at least three proteolytic activities including an extracellular serine protease. In general, serine proteases display a wide range of substrate specificities, which are believed to be mediated by an active site composed of one Asp, one His, and a Ser residue in the molecule. This enzyme prefers to hydrolyze peptide bonds on the carboxyl side of glutamic or aspartic acid._x000D_ Application_x000D_ Protease from Streptomyces griseus has been used:_x000D_ • for the digestion of nucleus pulposus (NP) tissue_x000D_ • in the catalysis of asymmetric one pot Mannich reaction_x000D_ • for deproteinization of starch_x000D_ • digestion of brain slices for the cell dissociation_x000D_ Protease is an enzyme used to break down proteins by hydrolyzing peptide bonds. Protease is used to degrade proteins, to study protease inhibitors and to study thermal inactivation kinetics. Protease is used in nucleic acid isolation procedures in incubations. Protease from Streptomyces griseus has been used in crystallographic and kinetic investigations of the covalent complex formed by tetrapeptide aldehydes and serine proteases._x000D_ Protease is typically used in nucleic acid isolation procedures in incubations of 0.5-3.0 hours supplemented with 0.2% sodium dodecyl sulfate and 10 mM EDTA._x000D_ The enzyme from Sigma has been used for the digestion and analysis of antithrombin-heparin complexes. It has also been used for the isolation of enzyme-resistant starch._x000D_ This enzyme is more active at a higher pH range than the known alkaline protease, showing the proteolytic activity even in 0.2N NaOH solution. This enzyme is useful for proteolysis of insoluble protein and for structure investigation of protein._x000D_ Packaging_x000D_ 1, 5 g in glass bottle_x000D_ 100 mg in glass bottle_x000D_ Biochem/physiol Actions_x000D_ Protease catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Protease from Streptomyces griseus is a mixture of at least three proteolytic activities including an extracellular serine protease. Serine proteases display a wide range of substrate specificities, which are believed to be mediated by an active site composed of one Asp, one His, and a Ser residue in the molecule. This enzyme prefers to hydrolyze peptide bonds on the carboxyl side of glutamic or aspartic acid._x000D_ This product is a mixture of at least three caseinolytic activities and one aminopeptidase activity. The caseinolytic enzymes were named as Streptomyces griseus Protease A, Streptomyces griseus Protease B and Streptomyces griseus Trypsin. This product may be used when extensive or complete degradation of protein is required. This protease mixture is highly nonspecific and can digest casein to the extent of >70% as mono-amino acids._x000D_ Features and Benefits_x000D_ • highly stable in pH range of 5.0 to 9.0, with peak activity at pH 8.8_x000D_ • compatible with many DNA and RNA isolation buffers_x000D_ • broad substrate specificity_x000D_ Quality_x000D_ Contains calcium acetate._x000D_ Physical properties_x000D_ Completely inactivated by heating above 80 °C for 15-20 minutes._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_ Preparation Note_x000D_ Collected from culture broth of S. griseus.