Synonym: Alkaline Protease, Protease from Bacillus licheniformis, Proteinase from Bacillus licheniformis, Subtilo peptidase A
|Related Categories||3.4.x.x Peptidases, 3.x.x.x Hydrolases, Analytical and Industrial Enzymes, Application Index, Biochemicals and Reagents,|
|activity||≤0.05 Kunitz units/mg solid RNase|
|≤5.0 Kunitz units/mg solid DNase|
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Amino acid analysis and isoelectric focusing electrophoresis consistent with subtilisin Carlsberg.
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.
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).
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 NHE11.
Proteinase catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphat
Subtilisin is a non-glycosylated single polypeptide chain without disulfide bonds and has a molecular weight of 27 KDa.
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Certificate of Analysis
Certificate of Origin
|Symbol||GHS05, GHS07, GHS08|
|Precautionary statements||P261-P280-P305 + P351 + P338-P342 + P311|
|Personal Protective Equipment||dust mask type N95 (US), Eyeshields, Faceshields, Gloves|
|Hazard Codes (Europe)||Xn|
|Risk Statements (Europe)||37/38-41-42|
|Safety Statements (Europe)||22-24-26-36/37/39|
1. OBJECTIVE To standardize a procedure for the enzymatic assay of Protease using Casein as a substrate at Sigma-Aldrich St. Louis.
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Keywords: Cell culture, Cell disruption, Cell signaling, Diagnostic, Digestions, Drug discovery, Functional genomics, Gene expression, Genomics, Metabolic Pathways, Molecular biology, Neuroscience, Proteomics
Comment on Enhancement of the catalytic activity of a 27 kDa subtilisin-like enzyme from Bacillus amyloliquefaciens CH51 by in vitro mutagenesis. Viqar B, Gopinath A, Dimitrov JD, et al. J. Agric. Food Chem. 60(16), 4170-2, (2012)
Discovery of a new role of human resistin in hepatocyte low-density lipoprotein receptor suppression mediated in part by proprotein convertase subtilisin/kexin type 9. Melone M, Wilsie L, Palyha O, et al. J. Am. Coll. Cardiol. 59(19), 1697-705, (2012)
Importance of tetrahedral intermediate formation in the catalytic mechanism of the serine proteases chymotrypsin and subtilisin. Petrillo T, O'Donohoe CA, Howe N, et al. Biochemistry 51(31), 6164-70, (2012)
NaStEP: a proteinase inhibitor essential to self-incompatibility and a positive regulator of HT-B stability in Nicotiana alata pollen tubes. Jiménez-Durán K, McClure B, García-Campusano F, et al. Plant Physiol. 161(1), 97-107, (2013)
Determination of the complete amino-acid sequence of subtilisin DY and its comparison with the primary structures of the subtilisins BPN', Carlsberg and amylosacchariticus. Nedkov P, Oberthür W, and Braunitzer G Biol. Chem. Hoppe-Seyler 366(4), 421-30, (1985)
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