You searched for: Enzymes

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The amount of macerating activity on potato tuber disks as determined by weight loss at 40 °C, pH 5,0.

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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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Collagenase can be solubilised in calcium-free solutions such as Hank's Balanced Salts or Earles Balanced Salt Solution.

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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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Catalase activates the decomposition of hydrogen peroxide, a reactive oxygen species, into water and oxygen.

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Dissolves readily at 5 mg/ml in 0,06 M Tris/HCI pH 7,4 to give a clear colorless solution.

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Lyophilised in vials containing approximately 5 mg dry wt. and at least 100 units/vial (20 to 40 units/mg dry wt.).

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Trypsin-EDTA solution is widely used for cell dissociation, routine cell culture passaging, and primary tissue dissociation due to its digestive strength.

Supplier: Cytiva

Thrombin is a protease used to digest fusion proteins prepared from pGEX vectors containing the recognition sequence for thrombin (pGEX-1lT, pGEX-2T, pGEX-2TK, pGEX-4T-1, pGEX-4T-2, and pGEX-4T-3).

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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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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Streptokinase catalyzes hydrolysis of amide linkages. Forms a 1:1 complex with plasminogen which is then converted to streptokinase-plasmin. Both streptokinase-plasminogen and streptokinase-plasmin complexes can activate plasminogen. As a result of its interaction with human or rabbit plasminogen, streptokinase undergoes specific fragmentation.

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Trichoderma reesei cellulase

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Yeast aldehyde dehydrogenase

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Recombinant Tobacco Etch Virus (from E. coli)

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Synthetic Yeast Inorganic Pyrophosphatase (from E. coli)

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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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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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Lysozyme (muramidase) hydrolyses preferentially the β-1,4 glucosidic linkages between N-acetylmuramic acid and N-acetylglucosamine which occur in the mucopeptide cell wall structure of certain microorganisms, such as Micrococcus lysodeikticus.

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Activators: Papain is activated by cysteine, sulphide, sulphite and more. It is enhanced when heavy metal binding agents such as EDTA are also present. N-bromosuccinimide enhances the activity. Inhibitors: Substances which react with sulphydryl groups including heavy metals, carbonyl reagents. Aldehydes are papain inhibitors. Benzoylamidoacetonitrile is an inhibitor. See Shapira and Arnon (1967a and b) on antibody inhibitors. Papain may be inactivated by H₂O₂ generated by γ-irradiation of H₂O⁻ the active SH group being oxidised to sulphenic acid. Specific inhibitors are AEBSF, antipain, cystatin, E-64, leupeptin, PMSF, TLCK and TPCK.

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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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One unit decomposes 1,0 µmole of hydrogen peroxide per minute at pH 7,0, 25 °C.

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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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Aspergillus niger Type X glucose oxidase

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CHOD is soluble in cold 50 mM potassium phosphate buffer, pH 7,0. Prepare solutions immediately before use.

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One unit will hydrolyse 1,0 µmole of o-nitrophenyl-beta-D-galactoside to o-nitrophenol per minute at pH 4,5 and 30 °C.

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One unit catalyses the liberation of 1 mmole reducing group (calculated as maltose per minute at pH 6,9 at 20 °C).