Vous avez recherché : Enzymes

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Collagenases degrade native helical collagen fibrils. The enzyme has an important role in connective tissue metabolism and is produced by specific cells involved in repairs and remodelling processes. It is a type II enzyme that contains greater clostripain activity. It is generally used for heart, bone, muscle, thyroid, cartilage, and liver cells. Ca²⁺ is required for its activation while metal chelating agents such as cysteine, EDTA or o-phenanthroline inhibits its activity.

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The hyaluronidase is purified from Streptomyces hyalurolyticus. This enzyme belongs to the endo-beta-hexosaminidase and endo-eliminase type enzyme that produces oligo-saccharide (unsaturated tetraose and pentose) by hydrolysing the beta-1,4-linkage of hyaluronic acid. It is stable in both high temperature and acid or alkaline range. It has high substrate specificity and hydrolyzes hyaluronic acid only in mucopolysaccharide.

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Pepsin is an acid protease, contains a proteolytic enzyme. It contains the "cathepsin" component which has milk curdling activity. It has a broad range of substrate activity and demonstrates an esterase acitivity. It generally attacks peptide bonds.

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Cellulase refers to a group of enzymes which, acting together, hydrolyse cellulose. The b-glucosidases, including cellobiose, are primarily active on the smaller molecular weight cellulose hydrolysates. During cellulose breakdown they are active on the dimers and oligomers of cellulose.

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Activity: Each vial contains 500 units β-Lactamase I and 50 units β-Lactamase II Unit Definition: One unit is defined as the amount of enzyme which will hydrolyse 1,0 micromole of benzyl penicillin and 1,0 micromole of cephalosporin C per minute at 25 °C in the presence of EDTA pH 7,0.

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Beta-glucuronidases are members of the glycosidase family of enzymes that catalyse breakdown of complex carbohydrates. Human β-glucuronidase is a type of glucuronidase that catalyses hydrolysis of β-D-glucuronic acid residues from the non-reducing end of mucopolysaccharides, such as heparan sulfate. In human gut β-glucuronidase converts conjugated bilirubin to the unconjugated form for reabsorption.

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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.

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HRP is a plant glycohemoprotein belongs to the ferroprotoporphyrin group of peroxidases. It is used in biochemistry applications such as western blots, ELISA and Immunohistochemistry. It is used to amplify a weak signal and increase detectability of a target molecule, such as a protein. HRP labeled immunoglobulins are used as probes for the demonstration of tissue antigens and in enzyme immunoassay (EIA) systems for determination of soluble and insoluble antigens.

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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.).

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Unit Definition: Enzyme activity is determined by a change in optical density in a solution of hyaluronic acid. Activity is compared to a hyaluronidase International Standard and is expressed as an International Unit (U).

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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.

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Suitable for both protein and nucleic acid isolation. Exhibits proteolytic activity on proteins, peptides, glycoproteins, amides and esters. Also active with nitroanilides of amino acids with protected amino groups, excluding arginine. Useful in the isolation of DNA and RNA, in the analysis of membrane structures and protein structure. Proteolytic activity: >30mAnson Units/mg Unit definition: One Anson unit is the amount of enzyme which liberates 1 µmol of Folin-positive amino acids per minute at pH 7,5 and 35 °C, using hemoglobin as substrate.

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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.

Supplier: MERCK PRODUCTION CHEMICALS

The best-in-class solution for nucleic acid removal at high salt concentration in Bioprocessing. The Benzonase® Salt Tolerant endonuclease Emprove® Expert is a new enzyme, different in amino acids sequence from other Benzonase® endonuclease references. It was designed with state-of-the-art protein engineering capabilities, to ensure the highest activity at high salt concentrations.

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Papain

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Trichoderma reesei cellulase

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Synthetic Yeast Inorganic Pyrophosphatase (from E. coli)

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Recombinant Tobacco Etch Virus (from E. coli)

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Recombinant Poly(A) Polymerase (from E. coli)

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Recombinant Alkaline Phosphatase (from E. coli)

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Diaphorase (from Clostridium kluyveri)

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Recombinant mRNA Cap 2'-O-methyltransferase (from E. coli)

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Synthetic Yeast Inorganic Pyrophosphatase (from E. coli)

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Yeast aldehyde dehydrogenase

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Chicken lysozyme (Muramidase) (from egg white)

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Aspergillus niger Type X glucose oxidase

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

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

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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: Abnova

Recombinant Alkaline Phosphatase (from E. coli)