You searched for: Enzymes

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

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: 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

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)

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.

Supplier: Merck

ADH (alcohol dehydrogenase) is a enzymes for biofuel cell research.

Supplier: Merck

Protease is an enzyme used to break down proteins by hydrolysing peptide bonds.

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.

Supplier: Merck

SOLu-Trypsin is an advanced proteomics grade enzyme that is solution stable for mass spectrometry. Recombinant, expressed in Pichia pastoris.

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.

Supplier: Merck

Cellulase, enzyme blend contains cellulases, ß-glucosidases, and hemicellulase, for the application of degrading cellulose to fermentable sugars.

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.

Supplier: Merck

The enzyme can be initially dissolved in 50 mM Hepes/KOH pH 7,4, 150 mM NaCl at 10 mg/ml.

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.

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.

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.

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.

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.

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.

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.

Supplier: Merck

Horseradish peroxidase, Typ I

Supplier: Merck

Aldehyde dehydrogenase (from Yeast)

Supplier: Merck

L-Lactate dehydrogenase Typ II (from Muscle)

Supplier: Merck

Ribonuclease A, type XII-A, from bovine pancreas.

Supplier: Merck

Hexokinase

Supplier: Merck

Xanthine oxidase from bovine milk, Grade I.

Supplier: Merck

Recombinant desoxyribonuclease I

Supplier: Merck

Yeast invertase

Supplier: Merck

L-Lactate dehydrogenase

Supplier: Merck

Horseradish peroxidase, Typ X