| Description | DescriptionClostripain also known as Clostridiopeptidase B or Endoproteinase Arg-C is a proteinase that cleaves peptide bonds on the carboxyl side of arginine. This protein is a heterodimer composed of a heavy and a light chain that are held together via strong noncovalent forces. As a proteolytic DescriptionClostripain also known as Clostridiopeptidase B or Endoproteinase Arg-C is a proteinase that cleaves peptide bonds on the carboxyl side of arginine. This protein is a heterodimer composed of a heavy and a light chain that are held together via strong noncovalent forces. As a proteolytic enzyme it can be used for isolation of various cell types by tissue dissociation.Clostripain exists in two different forms, an oxidized, native condition and a reduced activated form that differ in enzymatic activity. The native clostripain can be activated with reducing agents (e.g. DTT, Cysteine) resulting in a higher activity of the enzyme.ApplicationClostripain NB is used in combination with Collagenase NB 1 and/or Neutral Protease NB, suitable for cell isolation from various tissue types.SpecificationsContains chromatographically highly purified clostripain.Clostripain, native state activity: ≥ 5.0 U/mg (BAEE)Clostripain, activated activity: ≥ 50.0 U/mg (BAEE)Clostripain activity, native state, per vial: ≥ 200 U/vial (BAEE)Clostripain activity, activated, per vial: statusEC 3.4.24.3 • Mr ca. 59 000 • CAS [9028-00-6]References and DefinitionsUnit definition:Clostripain, native state (BAEE assay): 1 Unit catalyzes the cleavage of 1 µmol Nα-Benzoyl-L-arginine ethyl ester per minute at 25 °C, pH 7.8.Clostripain, activated (BAEE assay): 1 Unit catalyzes the cleavage of 1 µmol Nα-Benzoyl-L-arginine ethyl ester per minute at 25 °C, pH 7.8. The enzyme is activated with 2.5 mM DTT. References1. Bond, M.D. & van Wart, H.E. (1984) Biochemistry 23, 3077-30912. Kula et al. (1976) Biochem. Biophys. Res. Commun. 69, 389-396... Read More | Laccase is an enzyme, produced by ericoid mycorrhiza and ectomycorrhiza fungi. It belongs to the group of polyphenol oxidases. Laccase is also present in plants and bacteria.Laccase from Trametes versicolor has been used: to assess the use of four laccase-producing strains in waste water treatment Laccase is an enzyme, produced by ericoid mycorrhiza and ectomycorrhiza fungi. It belongs to the group of polyphenol oxidases. Laccase is also present in plants and bacteria.Laccase from Trametes versicolor has been used: to assess the use of four laccase-producing strains in waste water treatment in laccase assay in screening the lignolsSome of the enzymatic actions of laccase are associated with sporulation, detoxification, morphogenesis, melanin polymerization and it offers protection to spore coat. Laccase can catalyse a number of substrates including medicinal drugs and halogenated pesticides. It utilizes oxygen for its catalysis. For these reasons, it might be useful in the biological degradation of micropollutants in wastewater treatment. Laccase catalyzes the oxidation of phenol containing compounds, including lignin, through the reduction of oxygen to water. The presence of mediators will allow the oxidation of non-phenlic compounds as well. The primary function of laccase is to degrade lignin in fungi... Read More | Inquire | Product Application：Isoelectric point: 7.2 (Maehly 1955).Inhibitors: Horseradish peroxidase is reversibly inhibited by cyanide and sulfide at a concentration of 10-5 M (Theorell 1951).Specificity: The enzyme exhibits a high specificity. Activity is observed with H2O2, MeOOH, and EtOOH (MaehlyProduct Application：Isoelectric point: 7.2 (Maehly 1955).Inhibitors: Horseradish peroxidase is reversibly inhibited by cyanide and sulfide at a concentration of 10-5 M (Theorell 1951).Specificity: The enzyme exhibits a high specificity. Activity is observed with H2O2, MeOOH, and EtOOH (Maehly and Chance 1954). See also Chmielnicka et al. (1971) and Morrison and Bayse (1973)... Read More | Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino acid leader sequence resulting in the 23.8 kDa Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino acid leader sequence resulting in the 23.8 kDa trypsin molecule. The optimum pH is 8.0. Trypsin is inhibited by organophosphorus compounds such as diisopropylfluorophosphate and natural inhibitors from pancreas. Soybean, lima bean, and egg white are also sources of natural inhibitors. Trypsin cleaves amide and ester bonds of Arg and Lys. The Aladdin Sequencing Grade Trypsin has been further purified to remove trace contaminating proteases and autolysis products which could interfere in trypsin digestion experiments, and exhibits a single band on PAGE.Trypsin is a serine protease used to hydrolyze proteins. Trypsin from bovine pancreas has a molecular weight of 23.8 kDa. Trypsins are used for the re-suspension of cells during cell culture and in proteomics research for the digestion of various proteins... Read More |