You searched for: Enzymes
Enzymes accelerate, or catalyze, chemical reactions, and they are known to catalyze more than 5,000 biochemical reaction types. Most enzymes are proteins, although a few are catalytic RNA molecules. Choose specific enzymes for cleaving bonds, removing genomic DNA from RNA preparations, for producing fragments of proteins, or for use in ion exchange chromatography. Enzymes are used in the chemical industry and other industrial applications when extremely specific catalysts are required.
Alcohol dehydrogenase, MP Biomedicals
Supplier: MP Biomedicals
Dissolves readily at 5 mg/ml in 0,01 M Sodium Phosphate pH 7,5 to give a clear colourless solution.
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Sorbitol dehydrogenase, MP Biomedicals
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.
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illustra Exonuclease I
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.
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Alcaligenes sp. Choline Oxidase, MP Biomedicals
Supplier: MP Biomedicals
Activity: 10 units/mg solid or more (containing approx. 20% of stabilisers). Unit definition: One unit causes the formation of one micromole of hydrogen peroxide per minute at pH 8,0 at 37 °C. Ref.: P.J.G. Mann and J.H. Quastel, Biochem. J., 31: 869 (1937)
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Aldolase, MP Biomedicals
Supplier: MP Biomedicals
Aldolase is a tetrameric protein. It catalyses a key reaction in glycolysis and energy production:D-Fructose 1,6-bisphosphate aldolase → dihydroxyacetone phosphate + D-glyceraldehyde-3-phosphate. Aldolase is present in all animal tissue and in most microorganisms. There are two classes of aldolases. Class I aldolase is found in animal and higher plant tissue. Class II aldolase is found in primitrive cells such as yeasts and bacteria. Class I aldolase is characterised by not requiring a bivalent metal cofactor and the formation of a ketimine Schiff base intermediate with the substrate dihydroxyacetone phosphate. Class II aldolase requires a metal cofactor and is inhibited by EDTA. Three types of aldolase exist in animal tissue. The major form, type A is found in muscle; type B is found in liver tissue and type C (plus some type A) is found in brain tissue. Aldolase forms five isozymes which may to various degrees be organ specific.
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Alcohol dehydrogenase (from Saccharomyces cerevisiae)
Supplier: Merck
ADH (alcohol dehydrogenase) is a enzymes for biofuel cell research.
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Protease (from Bacillus licheniformis)
Supplier: Merck
Protease is an enzyme used to break down proteins by hydrolysing peptide bonds.
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Horse Butyrylcholinesterase (from Serum)
Supplier: Merck
Butyrylcholinesterase from equine serum has been used in a microcalorimetric study of the inhibition of butyrylcholinesterase by paraoxon. This enzyme has also been used in a study to investigate the synthesis and inhibition of cholinergic enzymes.
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Recombinant SOLu-trypsin (from P. pastoris)
Supplier: Merck
SOLu-Trypsin is an advanced proteomics grade enzyme that is solution stable for mass spectrometry. Recombinant, expressed in Pichia pastoris.
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Ascorbate oxidase (from Cucumis sp.)
Supplier: Merck
Ascorbate Oxidase is an enzyme belonging to the family of oxidoreductases that catalyses the reaction: Ascorbic acid + ½ O₂ ascorbate oxidase → Dehydroascorbic acid + H₂O.
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Cellulase
Supplier: Merck
Cellulase, enzyme blend contains cellulases, ß-glucosidases, and hemicellulase, for the application of degrading cellulose to fermentable sugars.
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Acetylcholinesterase
Supplier: Merck
Acetylcholinesterase from Electrophorus electricus is a tetramer composed of 4 equal subunits of 70 kDa each. Each subunit contains one active site. The enzyme is a glycoprotein containing hexosamines.
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Bacillus polymyxa Dispase II (from Bacillus polymyxa)
Supplier: Merck
The enzyme can be initially dissolved in 50 mM Hepes/KOH pH 7,4, 150 mM NaCl at 10 mg/ml.
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α-Amylase (from Aspergillus oryzae)
Supplier: Merck
Aspergillus oryzae α-amylase enzyme catalyzes the hydrolysis of the α-1,4 glycosidic bonds in soluble starches and related subsrates. These substrates are broken down to release short oligosaccharides and α-limit dextrins. Also act as control enzyme in agar plate-based and carboxymethylcellulose-based clearing assays to screen cellulase activity.
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Bovine Trypsin (from Pancreas)
Supplier: Merck
The trypsin molecule has two domains: one is related to the enzyme active site and the tryptophan residues; the other is related to the 8-anilinonaphthalene-1-sulfonate binding.
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Glucose-6-Phosphate Dehydrogenase
Supplier: Merck
Glucose-6-phosphate dehydrogenase is used to test ketose reductase activity in developing maize endosperm. It catalyses the conversion of glucose-6-phosphate to 6-phosphogluconolacetone as the first step in the pentose phosphate pathway. Also it is a key regulatory enzyme in the first step of the pentose phosphate pathway.
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Aldehyde dehydrogenase (from Yeast)
Supplier: Merck
Aldehyde dehydrogenase from baker′s yeast catalyses the reduction of pyridine nucleotides by several aldehydes. It catalyses the oxidation of a wide range of substrates, such as acetaldehyde, formaldehyde, propionaldehyde, n-butylaldehyde, isobutylaldehyde, n-valeraldehyde, caproaldehyde, benzaldehyde, glycoaldehyde, D-glyceraldehyde, malonic semialdehyde, and succinic aldehyde. The enzyme has been used to study the production of ethanol and isobutanol.
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Pronase E (from Streptomyces griseus)
Supplier: Merck
A mixture of at least three proteolytic activities including an extracellular serine protease. In general, serine proteases display a wide range of substrate specificities, which are believed to be mediated by an active site composed of one Asp, one His, and a Ser residue in the molecule. This enzyme prefers to hydrolyze peptide bonds on the carboxyl side of glutamic or aspartic acid.
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alpha-Chymotrypsin
Supplier: Merck
α-Chymotrypsin is a serine peptidase and has 241 amino acid residues contained in three polypeptide chains (A chain-13 residues, B chain-131 residues, and C chain-97 residues) linked by disulfide bridges. Molecular weight of this enzyme is found to be 25 kDa. Its pI is 8,75. It selectively hydrolyses peptide bonds on the C-terminal side of tyrosine, phenylalanine, tryptophan, and leucine. Ca²⁺ activates and stabilizes the enzyme. The enzyme is inhibited by diisopropyl fluorophosphate (DFP), phenylmethanesulfonyl fluoride (PMSF), N-p-tosyl-L-phenylalanine chloromethyl ketone (TPCK), chymostatin, aprotinin, α1-antitrypsin, α2-macroglobulin, 10 mM Cu²⁺ and Hg²⁺.A serine protease that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains (Tyr, Trp, Phe, Met, Leu) on the carboxyl end of the bond.
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alpha-Chymotrypsin
Supplier: Merck
Chymotrypsin (Chy) is a serine protease. It corresponds to a molecular weight of 25,7 kDa and is widely used in pharmaceutical industry.It is synthesized in pancreas from chymotrypsinogen and require calcium for this conversion.α-Chymotrypsin from bovine pancreas (bovine pancreatic α-chymotrypsin, CHT) is an enzyme protein.The influence of varying concentrations of organic solvents like ethanol, 1,4-dioxane and acetonitrile on CHT has been reported.
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Horseradish peroxidase, Typ I
Supplier: Merck
Horseradish peroxidase, Typ I
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Aldehyde dehydrogenase (from Yeast)
Supplier: Merck
Aldehyde dehydrogenase (from Yeast)
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L-Lactate dehydrogenase Typ II (from Muscle)
Supplier: Merck
L-Lactate dehydrogenase Typ II (from Muscle)
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Bovine Ribonuclease A (from Pancreas)
Supplier: Merck
Ribonuclease A, type XII-A, from bovine pancreas.
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Bovine Xanthine oxidase (from Milk)
Supplier: Merck
Xanthine oxidase from bovine milk, Grade I.
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Recombinant desoxyribonuclease I
Supplier: Merck
Recombinant desoxyribonuclease I
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Horseradish peroxidase, Typ X
Supplier: Merck
Horseradish peroxidase, Typ X