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.
Bovine alpha-Chymotripsin (from Pancreas), MP Biomedicals
Supplier: MP Biomedicals
Preparation Method
Produced from 3× crystallised chymotrypsinogen
α-Chymotrypsin is used for treating pancreatic insufficiency and in traumatology.
Chymotrypsin preferentially catalyses the hydrolysis of peptide bonds involving L-isomers of tyrosine, phenylalanine, and tryptophan. It also readily acts upon amides and esters of susceptible amino acids. In addition to bonds involving aromatic amino acids, chymotrypsin catalyses at a high rate the hydrolysis of bonds of leucyl, methionyl, asparaginyl, and glutamyl residues. a-Chymotrypsin is a protein consisting of 241 amino acid residues. The molecule has three peptide chains: an A chain of 13 residues, a B chain of 131 residues, and a C chain of 97 residues.
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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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Human Factor XIa
Supplier: Haematologic Technologies
Factor XIa is a serine protease which participates in the instrinsic pathway of coagulation by catalysing the conversion of factor IX to factor IXa.
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Human gamma-Thrombin
Supplier: Haematologic Technologies
Proteolysed forms of α-thrombin have been termed β-thrombin and γ-thrombin. β-thrombin is generated by cleavage of the A-chain of α-thrombin at Arg-13 and Lys-30, and cleavage of the B-chain at Lys-114 and Arg-122. γ-thrombin is generated from β-thrombin by an additional cleavage of the B-chain.
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Human alpha-Thrombin
Supplier: Haematologic Technologies
Alpha-thrombin is a highly specific serine protease. During coagulation, thrombin cleaves fibrinogen to form fibrin leading to the formation of a fibrin clot. Thrombin is also responsible for feedback activation of the procofactors factor V and factor VIII. Thrombin has also been reported to activate factor VIII and platelets, and also functions as a vasoconstrictor protein.
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Human beta-Thrombin
Supplier: Haematologic Technologies
Proteolysed forms of α-thrombin have been termed β-thrombin and γ-thrombin. β-thrombin is generated by cleavage of the A-chain of α-thrombin at Arg-13 and Lys-30, and cleavage of the B-chain at Lys-114 and Arg-122. γ-thrombin is generated from β-thrombin by an additional cleavage of the B-chain.
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Bovine alpha-Thrombin
Supplier: Haematologic Technologies
Alpha-thrombin is a highly specific serine protease. During coagulation, thrombin cleaves fibrinogen to form fibrin leading to the formation of a fibrin clot. Thrombin is also responsible for feedback activation of the procofactors factor V and factor VIII. Thrombin has also been reported to activate factor VIII and platelets, and also functions as a vasoconstrictor protein.
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Fructanase
Supplier: MEGAZYME
This purified fructanase mixture is used for the determination of fructn (liquid), in research, biochemical enzyme assays and in vitro diagnostic analysis.
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Trichoderma endo-1,3-beta-D-glucanase (from Trichoderma sp.)
Supplier: MEGAZYME
endo-1,3-β-D-Glucanase is isolated from Trichoderma species. These are used in carbohydrate and biofuels research, biochemical enzyme assays and in vitro diagnostic analysis.
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Linamarase (beta-D-Glucosidase)
Supplier: MEGAZYME
Linamarase (beta-D-Glucosidase)
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Bromelain (from stem)
Supplier: LGC Standards PROMOCHEM
Bromelain (from stem)
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Bovine alpha-Chymotrypsin (from Pancreas)
Supplier: LGC Standards PROMOCHEM
Bovine alpha-Chymotrypsin (from Pancreas)
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DENARASE® High Salt
Supplier: C LECTA
DENARASE High Salt is an engineered version of the wild-type Serratia marcescens endonuclease, which is commonly used for DNA removal applications in bioprocessing. Compared to the wild-type DENARASE, a few amino acids were substituted to provide the enzyme with an improved salt tolerance without losing its specificity for nucleic acids.
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exo-1,3-β-D-Glucanase + β-Glucosidase
Supplier: MEGAZYME
High purity exo-1,3-β-D-Glucanase (Trichoderma sp.) + β-Glucosidase (Aspergillus niger) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.
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Pronase E (from Streptomyces griseus)
Supplier: Serva
Pronase E (from Streptomyces griseus)
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Tritirachium album proteinase K
Supplier: Serva
Tritirachium album proteinase K
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Tritirachium album proteinase K
Supplier: Roth Carl
Tritirachium album proteinase K
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Bovine trypsin (from pancreas)
Supplier: Serva
Bovine trypsin (from pancreas)
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Bovine desoxyribonuclease I (from Pancreas)
Supplier: Serva
Bovine desoxyribonuclease I (from Pancreas)