Sie haben gesucht nach: Enzymes

Supplier: MP Biomedicals

Catalase activates the decomposition of hydrogen peroxide, a reactive oxygen species, into water and oxygen.

Supplier: MP Biomedicals

Soluble in distilled water or dilute buffer; dissolves readily at 5 mg/ml in 0,1 M potassium phosphate pH 7,4.

Supplier: MP Biomedicals

Dissolves readily at 5 mg/ml in 0,06 M Tris/HCI pH 7,4 to give a clear colorless solution.

Supplier: MP Biomedicals

Alkaline phosphatase is a phosphomonoesterase, used to remove 5′-phosphate groups from nucleic acid molecules to prevent self-ligation of DNA fragments and vectors during recombinant DNA manipulations.

Supplier: MP Biomedicals

Creatinine deiminase has been used in a study to assess the application of a creatinine-sensitive biosensor for hemodialysis control. It has also been used in a study to investigate the bioelectronic tongue for the simultaneous determination of urea, creatinine and alkaline ions in clinical samples.

Supplier: MP Biomedicals

Protease isolated from S. aureus, strain V8, this protease exhibits cleavage of peptide bonds on the COOH-terminal side of either aspartate or glutamate residues.

Supplier: MP Biomedicals

Dissolves readily at 5 mg/ml in 0,01 M Sodium Phosphate pH 7,5 to give a clear colourless solution.

Supplier: MP Biomedicals

Dissolves readily at 5 mg/ml in 0,05 M sodium/potassium phosphate pH 7,0 giving a clear green solution.

Supplier: MP Biomedicals

Dissolves readily at 5 mg/ml in 0,05 M sodium/potassium phosphate pH 7,0 giving a clear green solution.

Supplier: MP Biomedicals

Hyaluronidase is a glycoprotein containing 5% mannose and 2,17% glucosamine, it catalyses the random hydrolysis of 1,4-linkages between 2-acetamido- 2-deoxy- b-D-glucose and D-glucose residues in hyaluronate. Hyaluronidase from bovine testes is a tetramer consisting of 4 equal subunits with a molecular mass of 14 kDa each.

Supplier: MP Biomedicals

Glycerol-3-phosphate oxidase has been used for sensitive metabolite assays of starch and lipid synthesis, pyrophosphate, ATP, ADP, and most glycolytic intermediates in Arabidopsis seeds. It is a part of the dihydroxyacetone phosphate:glycerol-3-phosphate cycle in the bloodstream form of Trypanosoma brucei.

Supplier: MP Biomedicals

Trypsin consists of a single chain polypeptide of 223 amino acid residues. It is a member of the serine protease family. It composed of two subunits, α-trypsin and β-trypsin. α-Trypsin is composed of two peptide chains and β-trypsin is composed of one chain.

Supplier: MP Biomedicals

Activators: Ca²⁺ is required. Inhibitors: Metal chelating agents such as cysteine, EDTA or o-phenanthroline but not DFP. It is also inhibited by a2-macroglobulin - a large plasma glycoprotein. The human skin enzyme is inhibited by human serum but granulocyte collagenase is not. Human serum contains a2-macroglobulin and a1-antitrypsin that may inhibit certain collagenases.

Supplier: MP Biomedicals

Pectolyase Y-23 contains two types of pectinase such as endopolygalacturonase and endo-pectin lyase in high activity. It includes maceration stimulating factor which stimulates tissue maceration by both pectinases.

Supplier: MP Biomedicals

One unit will oxidise 1,0 µmole of formaldehyde to formic acid per minute at pH 7,5 and 37 °C.

Supplier: MP Biomedicals

Lyophilised in vials containing approximately 5 mg dry wt. and at least 100 units/vial (20 to 40 units/mg dry wt.).

Supplier: MP Biomedicals

Soluble in distilled water. Soluble in 0,1 M potassium phosphate buffer, pH 6,0 (monobasic potassium phosphate adjusted to pH 6,0 with 1,0 M potassium hydroxide) (10 mg/ml yields a clear, red-brown solution). Solutions of HRP can be kept refrigerated for up to a year while maintaining practically undiminished activity. Optimal pH is 6,0 to 6,5 (activity at pH 7,5 is 84% of the maximum). The enzyme is most stable in the pH range of 5,0 to 9,0 (Lit.).

Supplier: MP Biomedicals

Sorbitol dehydrogenase has been used in a study to investigate osmotic stress induced oxidative damage as a possible mechanism of cataract formation in diabetes.

Supplier: MERCK PRODUCTION CHEMICALS

Benzonase® is a highly active nuclease that degrades DNA and RNA to short oligonucleotides. It is used for the elimination of interfering DNA/RNA, for example at protein isolation, or before electrophoresis or chromatography.

Supplier: MERCK PRODUCTION CHEMICALS

Pancreatin 1400 FIP-U/g Protease, 24000 FIP-U/g Lipase, 30000 FIP-U/g Amylase EMPROVE® exp Ph. Eur., USP, ESSENTIAL

Supplier: MP Biomedicals

Horseradish peroxidase (HRP) is isolated from horseradish roots and belongs to the ferroprotoporphyrin group of peroxidases. It is a single chain polypeptide containing four disulfide bridges. It is a glycoprotein containing 18% carbohydrate. The carbohydrate composition consists of galactose, arabinose, xylose, fucose, mannose, mannosamine, and galactosamine depending upon the specific isozyme.

Supplier: MP Biomedicals

Catalase, fungal suspension from from Aspergillus niger is long-acting, extremely stable form of catalase that is active over a wide pH range. Composed of four protein subunits, each containing a heme group bound to its active site.

Supplier: MP Biomedicals

Trypsin-EDTA solution is widely used for cell dissociation, routine cell culture passaging, and primary tissue dissociation due to its digestive strength.

Supplier: Cytiva

Thrombin is a protease used to digest fusion proteins prepared from pGEX vectors containing the recognition sequence for thrombin (pGEX-1lT, pGEX-2T, pGEX-2TK, pGEX-4T-1, pGEX-4T-2, and pGEX-4T-3).

Supplier: MP Biomedicals

Lysozyme (muramidase) hydrolyses preferentially the β-1,4 glucosidic linkages between N-acetylmuramic acid and N-acetylglucosamine which occur in the mucopeptide cell wall structure of certain microorganisms, such as Micrococcus lysodeikticus.

Supplier: MP Biomedicals

Acetyl-CoA is produced via beta-oxidation of fatty acids, via the metabolism of carbohydrates - glucose 6-phosphate to pyruvate to acetyl-CoA and via the catabolism of amino acids. Acetyl-CoA has a number of metabolic opportunities. It is metabolised in the tricarboxylic acid cycle to produce carbon dioxide, water and energy.

Supplier: MP Biomedicals

Streptokinase catalyzes hydrolysis of amide linkages. Forms a 1:1 complex with plasminogen which is then converted to streptokinase-plasmin. Both streptokinase-plasminogen and streptokinase-plasmin complexes can activate plasminogen. As a result of its interaction with human or rabbit plasminogen, streptokinase undergoes specific fragmentation.

Supplier: MP Biomedicals

Proteinase K is a highly active stable endopeptidase with a broad spectrum of action was isolated by E. Merk's Darmstadt Biochemical Research Department in 1970 from a culture filtrate of the fungus, Tritirachium album Limber. This fungus is able to grow on Keratin (e.g., wool, horn particles) as the sole source of carbon and nitrogen. The isolated protease was, therefore, given the K designation.
Proteinase K is a stable and highly reactive serine protease. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active-site catalytic triad (Asp39-His69-Ser224). It is stable in a broad range of environments: pH, buffer salts, detergents (SDS), and temperature. In the presence of 0,1 to 0,5% SDS, proteinase K retains activity and will digest a variety of proteins and nucleases in DNA preparations without compromising the integrity of the isolated DNA.

Supplier: Cytiva

Exonuclease I acts specifically on single-stranded DNA degrading it processively in the 3'- to 5'-direction, producing 5'-mononucleotides. Applications include eliminating residual single-stranded DNA containing a 3'-terminus, measuring endonucleolytic cleavage of covalently closed circular (ccc) ssDNA, measuring DNA helicase activity.

Supplier: MP Biomedicals

Neuraminidase (Sialidase: Acylneuraminyl hydrolase; EC 3.2.1.18) From Arthrobacter ureafaciens lyophilised powder with salts. The salts are composed of sodium-potassium phosphate to give a solution of 10 mM phosphate buffer (pH 7) when enzyme is reconstituted with water to make activity of 1 unit per ml. Activity: >60 units/mg protein for NAN-lactose >25 units/mg protein for bovine submaxillary mucin >20 units/mg protein for colominic acid Protein is determined by the method of Lowry et al. with bovine albumin as a standard.6 Unit definition: One unit will liberate 1,0 µmole of N-acetyl-neuraminic acid (NANA) per minute at pH 5,0 at 37 °C, using either one NAN-lactose, bovine submaxillary mucin, or colominic acid as a substrate.