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.
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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Perfringolysin O, Recombinant, Clostridium Perfringens, aa29-500, His-Tag (PFO)
Supplier: US Biological
Perfringolysin O, Recombinant, Clostridium Perfringens, aa29-500, His-Tag (PFO)
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Human Plasminogen, MP Biomedicals
Supplier: MP Biomedicals
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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Amylase, MP Biomedicals
Supplier: MP Biomedicals
The number of grams of soluble starch dextrinized in the presence of excess B-amylase per hour at 40 °C, pH 5,0.
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Bovine trypsin (from pancreas), MP Biomedicals
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.
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L-Glutamic dehydrogenase, MP Biomedicals
Supplier: MP Biomedicals
For Continuous Spectrophotometric Rate determination method: 0,3 to 0,6 unit/ml of L-Glutamic dehydrogenase in cold Triethanolamine buffer.
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Protocatechuate-3,4-dioxygenase, MP Biomedicals
Supplier: MP Biomedicals
Inhibitors : Ag⁺, Hg²⁺, PCMB; Optimum temperature: 60 to 65 °C; Thermal stability: below 50 °C (pH 6,0; 1 h).
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Acetyl coenzyme A trilithium salt trihydrate, MP Biomedicals
Supplier: MP Biomedicals
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.
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alpha-Chymotrypsin, MP Biomedicals
Supplier: MP Biomedicals
One unit will hydrolyse 1,0 µmole of N-benzoyl-L-tyrosine ethyl ester (BTEE) per minute at pH 7,8 and 25 °C in the presence of ionised calcium.
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Lipase, MP Biomedicals
Supplier: MP Biomedicals
One USP unit of lipase activity is contained in the amount of pancreatin that liberates 1,0 µEq of acid per minute at a pH of 9,0 at 37 °C under the conditions of the assay for lipase activity.
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Sheep Hyaluronidase (from Testes), MP Biomedicals
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.
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Microbe creatinine deiminase, MP Biomedicals
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.
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Streptococcus sp. glycerol-3-phosphate oxidase, MP Biomedicals
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.
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Bovine hyaluronidase (from Testes), MP Biomedicals
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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beta-Galactosidase, MP Biomedicals
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.).
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Yeast aldehyde dehydrogenase, MP Biomedicals
Supplier: MP Biomedicals
Yeast aldehyde dehydrogenase
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Synthetic Yeast Inorganic Pyrophosphatase (from E. coli)
Supplier: Abnova
Synthetic Yeast Inorganic Pyrophosphatase (from E. coli)
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Recombinant Tobacco Etch Virus (from E. coli)
Supplier: Abnova
Recombinant Tobacco Etch Virus (from E. coli)
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Catalase, MP Biomedicals
Supplier: MP Biomedicals
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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Benzonase®
Supplier: MERCK PRODUCTION CHEMICALS
Benzonase® is a highly active nuclease that degrades DNA and RNA to short oligonucleotides. It is used for the elimination of interfering DNA/RNA, for example at protein isolation, or before electrophoresis or chromatography.
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Chicken lysozyme (from egg white), MP Biomedicals
Supplier: MP Biomedicals
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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Papain, MP Biomedicals
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.
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Tritirachium album proteinase K, MP Biomedicals
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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Neuraminidase, MP Biomedicals
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.
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Invertase
Supplier: MERCK PRODUCTION CHEMICALS
Humectants for confectionery