You searched for: Enzymes

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Ascorbate Oxidase is an enzyme belonging to the family of oxidoreductases that catalyses the reaction: Ascorbic acid +¹/₂ O₂ ascorbate oxidase → Dehydroascorbic acid +H₂O.

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One bacterial amylase unit is defined as that quantity of enzyme which will dextrinise one milligram of starch per minute at pH 6,6 and 30 °C.

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Alkaline phosphatase is a hydrolase enzyme responsible for removing phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids.

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For typical assay, dissolve enzyme at a concentration of 1 mg/ml in 0,05 M TES with 0,36 mM calcium chloride, pH 7,5. Dilutions run are 1/10 and 1/20 in the above buffer.

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Pancreatin are natural chemicals that help break down fats, proteins, and carbohydrates. Pancreatin is a digestive enzyme produced by the pancreas and delivered to the small intestine for the hydrolysis of complex nutrients.

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Zymolyase-20T is an enzyme preparation from a submerged culture of Arthrobacter luteus which effectively lyses cell walls of viable yeast cells. The primary enzyme in this preparation responsible for lysis of viable yeast cells is ß-1,3-glucan laminaripentaohydrolase. It hydrolyzes glucose polymers at the ß-1,3-glucan linkages releasing laminaripentaose as the principal product.

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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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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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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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Bromelain is a glycoprotein which is a highly active thiol proteinase (non-specific cysteine protease), which splits glycine esters but not lysine esters; it is also a protein-digesting and milk-clotting enzyme. Substrates susceptible to bromelain include all of the common protein materials such as gelatin, casein, gluten, collagen, elastin, globulins an muscle fiber protein. It is a cysteine endopeptidase with broad specificity for cleavage of proteins. It may be from a stem or piece of fruit.

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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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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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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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Protease

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Benzonase®

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Glutathione S-Transferase

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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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Pig Trypsin (from Pancreas)

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Stable powder 3X

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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.

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Dissolves readily at 2 mg/ml in analytical grade water to give a clear colorless solution.

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DIASTASE from malt, 1X N.F. stable, 60 mesh powder. Ready for CE IVD labeling of clinical applications.

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Cellulase Y-C removes cell walls from plant tissues in shorter incubation period without loss of biological activity of the materials.

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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.

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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.