| Description | Product Characteristics HRP-StabilPLUS is used for the dilution and stabilization of Horseradish Peroxidase (HRP) labeled proteins and antibodies, in order to maintain the molecular conformation and prevent loss of activity over time. This enables the making of re-diluted, ready-to-use HRP-Product Characteristics HRP-StabilPLUS is used for the dilution and stabilization of Horseradish Peroxidase (HRP) labeled proteins and antibodies, in order to maintain the molecular conformation and prevent loss of activity over time. This enables the making of re-diluted, ready-to-use HRP-conjugates, minimizing assay errors in dilution. Superior stabilization of HRP conjugated antibodies in low as well as high protein dilutions is seen, when using HRP-StabilPLUS. Diluted HRPconjugated proteins display stability as follows:• at least 4 years at 2-8 °C • at least 2 years at room temperature • at least 10 weeks at 37 °C.Composition & Properties HRP-StabilPLUS is a ready-to-use buffer that appears as a slightly white solution. The product is based on a mild acid Tris buffer containing proprietary stabilizing components. HRP-StabilPLUS contains neither BSA, nor other material from bovine serum, azide, mercury or other toxic components.Working Procedure 1.Make a series of dilutions of the HRP-conjugated protein in HRP-StabilPLUS in order to determine the optimal dilution. 2.Run the assay as usual or store the diluted HRPconjugated protein preferably at 2-8 °C.Tips & Tricks • HRP-StabilPLUS cannot be used for the dilution of antibodies directed against rabbit immunoglobulins i.e. Swine anti-Rabbit Ig & Goat anti-Rabbit Ig etc. UNI-StabilPLUS (cat. no. U494463) is recommended for this purpose.Handling & Storage • Store solution at 2-8 °C... Read More | Inquire | Collagenase NB 1 is chromatographically highly purified; therefore it contains a very high collagenolytic activity. It is largely free from additional enzymatic activities like clostripain, trypsin-like activity and neutral protease, as well as endotoxins.SpecificationsContains chromatographically Collagenase NB 1 is chromatographically highly purified; therefore it contains a very high collagenolytic activity. It is largely free from additional enzymatic activities like clostripain, trypsin-like activity and neutral protease, as well as endotoxins.SpecificationsContains chromatographically highly purified class I and class II collagenase (1).Largely free from clostripain, trypsin-like protease and neutral protease.Vial contains not less than 2000 PZ U collagenase.Activity (Wünsch): ≥ 3.00 U/mgEndotoxin: ≤ 10.0 EU/mg (Ph. Eur.)(Clostridiopeptidase A)EC 3.4.24.3 • Mr ca. 70 000 - 120 000 (collagenases) • CAS [9001-12-1]ApplicationCollagenase NB 1 is, mostly in combination with Neutral Protease NB, suitable for cell isolation from several tissue types.References and DefinitionsUnit definition: Collagenase: 1 U according to Wünsch (2) catalyzes the hydrolysis of 1 µmole 4-phenylazobenzyloxycarbonyl-L-prolyl-L-leucylglycyl-L-prolyl-D-arginine per minute at 25 °C, pH 7.1.Endotoxin: Ph. Eur. (1 Endotoxin Unit is equal to 1 International Unit of a WHO approved reference standard endotoxin (RSE)).References1. Bond, M.D. & van Wart, H.E. (1984) Biochemistry 23, 3077-30912. Wünsch, E. & Heidrich, H.G. (1963) Hoppe-Seyler's Z. Physiol. Chem. 333, 149-51... Read More | Format:10X ConcentrateProtein:Casein | Tyrosine decarboxylase catalyzes the removal of the carboxyl group from tyrosine to produce tyramine and carbon dioxide. Pyridoxal 5'-phosphate is a necessary cofactor. By using the apoenzyme prepared from cells grown on a vitamin B6 deficient medium pyridoxal phosphate may be determined. The Tyrosine decarboxylase catalyzes the removal of the carboxyl group from tyrosine to produce tyramine and carbon dioxide. Pyridoxal 5'-phosphate is a necessary cofactor. By using the apoenzyme prepared from cells grown on a vitamin B6 deficient medium pyridoxal phosphate may be determined. The HOLOenzyme may be used to determine tyrosine, phenylalanine and dihydroxyphenylalanine either manometrically or colorimetrically.L-Tyrosine decarboxylase apoenzyme from Streptococcus faecalis has been used in a study to purify and characterize tyrosine decarboxylase and aromatic-L-amino-acid decarboxylase.L-Tyrosine decarboxylase apoenzyme from Streptococcus faecalis has also been used in a study to investigate the stereospecificity of sodium borohydride reduction of tyrosine decarboxylase... Read More |