You searched for: Enzymes

Supplier: MP Biomedicals

Cellulase refers to a group of enzymes which, acting together, hydrolyse cellulose. The b-glucosidases, including cellobiose, are primarily active on the smaller molecular weight cellulose hydrolysates. During cellulose breakdown they are active on the dimers and oligomers of cellulose.

Supplier: Abnova

Collagenases are enzymes that break the peptide bonds in collagen.

Supplier: MP Biomedicals

Activity: Each vial contains 500 units β-Lactamase I and 50 units β-Lactamase II Unit Definition: One unit is defined as the amount of enzyme which will hydrolyse 1,0 micromole of benzyl penicillin and 1,0 micromole of cephalosporin C per minute at 25 °C in the presence of EDTA pH 7,0.

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Zymolyase-20T is an enzyme preparation from a submerged culture of Arthrobacter luteus which effectively lyses cell walls of viable yeast cells. The primary enzyme in this preparation responsible for lysis of viable yeast cells is ß-1,3-glucan laminaripentaohydrolase. It hydrolyzes glucose polymers at the ß-1,3-glucan linkages releasing laminaripentaose as the principal product.

Supplier: MP Biomedicals

Ascorbate Oxidase is an enzyme belonging to the family of oxidoreductases that catalyses the reaction: Ascorbic acid +¹/₂ O₂ ascorbate oxidase → Dehydroascorbic acid +H₂O.

Supplier: MP Biomedicals

Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) is a cytosolic enzyme in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH).

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Bromelain is a glycoprotein which is a highly active thiol proteinase (non-specific cysteine protease), which splits glycine esters but not lysine esters; it is also a protein-digesting and milk-clotting enzyme. Substrates susceptible to bromelain include all of the common protein materials such as gelatin, casein, gluten, collagen, elastin, globulins an muscle fiber protein. It is a cysteine endopeptidase with broad specificity for cleavage of proteins. It may be from a stem or piece of fruit.

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Pepsin is an acid protease, contains a proteolytic enzyme. It contains the "cathepsin" component which has milk curdling activity. It has a broad range of substrate activity and demonstrates an esterase acitivity. It generally attacks peptide bonds.

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

Collagenases degrade native helical collagen fibrils. The enzyme has an important role in connective tissue metabolism and is produced by specific cells involved in repairs and remodelling processes. It is a type II enzyme that contains greater clostripain activity. It is generally used for heart, bone, muscle, thyroid, cartilage, and liver cells. Ca²⁺ is required for its activation while metal chelating agents such as cysteine, EDTA or o-phenanthroline inhibits its activity.

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The hyaluronidase is purified from Streptomyces hyalurolyticus. This enzyme belongs to the endo-beta-hexosaminidase and endo-eliminase type enzyme that produces oligo-saccharide (unsaturated tetraose and pentose) by hydrolysing the beta-1,4-linkage of hyaluronic acid. It is stable in both high temperature and acid or alkaline range. It has high substrate specificity and hydrolyzes hyaluronic acid only in mucopolysaccharide.

Supplier: Abnova

Trichoderma reesei cellulase

Supplier: MP Biomedicals

Yeast aldehyde dehydrogenase

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Synthetic Yeast Inorganic Pyrophosphatase (from E. coli)

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Recombinant Tobacco Etch Virus (from E. coli)

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HRP is a plant glycohemoprotein belongs to the ferroprotoporphyrin group of peroxidases. It is used in biochemistry applications such as western blots, ELISA and Immunohistochemistry. It is used to amplify a weak signal and increase detectability of a target molecule, such as a protein. HRP labeled immunoglobulins are used as probes for the demonstration of tissue antigens and in enzyme immunoassay (EIA) systems for determination of soluble and insoluble antigens.

Supplier: MP Biomedicals

Dissolves readily at 5 mg/ml in 0,05 M sodium/potassium phosphate pH 7,0 giving a clear green solution.

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.

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.

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

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

Supplier: MP Biomedicals

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).

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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: 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.

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

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

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.).