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

Trypsin 1:250 from pig pancreas is used to release adherent cells from tissue culture plates for passaging. It was used in the isolation and culture of human endothelial cells.

Supplier: MP Biomedicals

Collagenase is a protease which cleaves the triple-helical protein called collagen. It has extensive use in biological studies, where it is used to prepare isolated cell suspensions.

Supplier: MERCK PRODUCTION CHEMICALS

Pancreatin 1400 FIP-U/g Protease, 24000 FIP-U/g Lipase, 30000 FIP-U/g Amylase EMPROVE® exp Ph. Eur., USP, ESSENTIAL

Supplier: MP Biomedicals

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

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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.

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: MP Biomedicals

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.

Supplier: MP Biomedicals

Catalase, fungal suspension from from Aspergillus niger is long-acting, extremely stable form of catalase that is active over a wide pH range. Composed of four protein subunits, each containing a heme group bound to its active site.

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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.

Supplier: MP Biomedicals

Acid phosphatase (APase) non-specifically catalyses the hydrolysis of monoesters and anhydrides of phosphoric acid to produce inorganic phosphate. It is used to study the production, transport, and recycling of phosphate and the metabolic and energy transduction processes of the cell.

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Plasminogen is a single-chain glycoprotein found in human plasma and extracellular fluid. Certain activators, such as tissue plasminogen activator (tPA), convert plasminogen to its active form, plasmin. Plasminogen has been used to study its conversion into plasmin.

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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.).

Supplier: MP Biomedicals

Horseradish peroxidase (HRP) is isolated from horseradish roots and belongs to the ferroprotoporphyrin group of peroxidases. It is a single chain polypeptide containing four disulfide bridges. It is a glycoprotein containing 18% carbohydrate. The carbohydrate composition consists of galactose, arabinose, xylose, fucose, mannose, mannosamine, and galactosamine depending upon the specific isozyme.

Supplier: MP Biomedicals

Trypsin consists of a single chain polypeptide of 223 amino acid residues. It is a member of the serine protease family. It composed of two subunits, α-trypsin and β-trypsin. α-Trypsin is composed of two peptide chains and β-trypsin is composed of one chain.

Supplier: MP Biomedicals

Creatinine deiminase has been used in a study to assess the application of a creatinine-sensitive biosensor for hemodialysis control. It has also been used in a study to investigate the bioelectronic tongue for the simultaneous determination of urea, creatinine and alkaline ions in clinical samples.

Supplier: MP Biomedicals

Hyaluronidase is a glycoprotein containing 5% mannose and 2,17% glucosamine, it catalyzes the random hydrolysis of 1,4-linkages between 2-acetamido- 2-deoxy- b-D-glucose and D-glucose residues in hyaluronate. It is a tetramer consisting of 4 equal subunits with a molecular mass of 14 kDa each.

Supplier: MP Biomedicals

Glycerol-3-phosphate oxidase has been used for sensitive metabolite assays of starch and lipid synthesis, pyrophosphate, ATP, ADP, and most glycolytic intermediates in Arabidopsis seeds. It is a part of the dihydroxyacetone phosphate:glycerol-3-phosphate cycle in the bloodstream form of Trypanosoma brucei.

Supplier: MP Biomedicals

Hyaluronidase is a glycoprotein containing 5% mannose and 2,17% glucosamine, it catalyses the random hydrolysis of 1,4-linkages between 2-acetamido- 2-deoxy- b-D-glucose and D-glucose residues in hyaluronate. Hyaluronidase from bovine testes is a tetramer consisting of 4 equal subunits with a molecular mass of 14 kDa each.

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Acetyl-CoA is produced via beta-oxidation of fatty acids, via the metabolism of carbohydrates - glucose 6-phosphate to pyruvate to acetyl-CoA and via the catabolism of amino acids. Acetyl-CoA has a number of metabolic opportunities. It is metabolised in the tricarboxylic acid cycle to produce carbon dioxide, water and energy.

Supplier: MP Biomedicals

Proteinase K is a highly active stable endopeptidase with a broad spectrum of action was isolated by E. Merk's Darmstadt Biochemical Research Department in 1970 from a culture filtrate of the fungus, Tritirachium album Limber. This fungus is able to grow on Keratin (e.g., wool, horn particles) as the sole source of carbon and nitrogen. The isolated protease was, therefore, given the K designation.
Proteinase K is a stable and highly reactive serine protease. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active-site catalytic triad (Asp39-His69-Ser224). It is stable in a broad range of environments: pH, buffer salts, detergents (SDS), and temperature. In the presence of 0,1 to 0,5% SDS, proteinase K retains activity and will digest a variety of proteins and nucleases in DNA preparations without compromising the integrity of the isolated DNA.

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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.

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

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.

Supplier: MP Biomedicals

Deoxyribonuclease from beef pancreas, DNase I, was first crystallized by Kunitz. It is an endonuclease which splits phosphodiester linkages, preferentially adjacent to a pyrimidine nucleotide yielding 5'-phosphate terminated polynucleotides with a free hydroxyl group on position 3'. The average chain of limit digest is a tetranucleotide. DNase I acts upon single chain DNA, and upon double-stranded DNA and chromatin.

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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Inhibitors: p-Chloromercuribenzoate, iodoacetamide, heavy metal ions (Zn²⁺, Fe²⁺, Zn²⁺, Cd²⁺, Cu²⁺, Pb²⁺, Ag⁺, Hg²⁺), ionic Detergents (SDS, DAC, etc.). Contaminants: The preparation is practically free from other glycosidases (a-galactosidase, a-,b-glucosidase, a-,b-mannosidase, etc.) and proteinase. Principle: o-Nitrophenyl-b-D-galactopyranoside (ONPG) b-galactosidase > o-Nitrophenol (ONP) + D-Galactose. The appearance of o-nitrophenol is measured at 410 nm by spectrophotemetry. Thermal Stability: Below 50 °C (pH 7,3; 15 min) (Lit.), Optimum Temperature: 50 to 55 °C (Lit.).

Supplier: MP Biomedicals

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.

Supplier: MP Biomedicals

Inhibitors: p-Chloromercuribenzoate, lodoacetamide, heavy metal ions (Zn²⁺, Fe²⁺, Zn²⁺, Cd²⁺, Cu²⁺, Pb²⁺, Ag⁺, Hg²⁺), Ionic Detergents (SDS, DAC, etc.). Contaminants: The preparation is practically free from other glycosidases (a-galactosidase, a-,b-glucosidase, a-,b-mannosidase, etc.) and proteinase. Principle: o-Nitrophenyl-b-D-galactopyranoside (ONPG) b-galactosidase > o-Nitrophenol (ONP) +D-Galactose. The appearance of o-nitrophenol is measured at 410 nm by spectrophotemetry. Thermal stability: below 50 °C (pH 7,3; 15 min) (Lit.), Optimum Temperature: 50 to 55 °C (Lit.).

Supplier: MP Biomedicals

Elastase is prepared from porcine pancreas. It is lyophilised and water soluble. Elastase is chromatographically prepared by the method of Narayanan and Anwar. In the method, 2 times crystalline elastase is adsorbed on a column of DEAE-Sephadex A50 to separate elastase and non-specific protein components. The elastase component is further purified by chromatography on a column of CM-Cellulose using a sodium chloride gradient to elute the elastase. The latter is dialysed until chloride-free and then lyophilised. During its preparation the elastase is held below a pH of 5,5 for greater than 24 hours. Two times crystallised from the euglobin fraction of porcine pancreas by the method of Lewis et al. Does not contain trypsin or chymotrypsin.