You searched for: Enzymes

Supplier: MP Biomedicals

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

Beta-glucuronidases are members of the glycosidase family of enzymes that catalyse breakdown of complex carbohydrates. Human β-glucuronidase is a type of glucuronidase that catalyses hydrolysis of β-D-glucuronic acid residues from the non-reducing end of mucopolysaccharides, such as heparan sulfate. In human gut β-glucuronidase converts conjugated bilirubin to the unconjugated form for reabsorption.

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

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: 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

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

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.

Supplier: MP Biomedicals

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

Supplier: MP Biomedicals

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.

Supplier: MP Biomedicals

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

Supplier: Abnova

Staphylococcus aureus Staphylokinase

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: Abnova

Recombinant mRNA Cap 2'-O-methyltransferase (from E. coli)

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: US Biological

Perfringolysin O, Recombinant, Clostridium Perfringens, aa29-500, His-Tag (PFO)

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.

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

For Continuous Spectrophotometric Rate determination method: 0,3 to 0,6 unit/ml of L-Glutamic dehydrogenase in cold Triethanolamine buffer.

Supplier: MP Biomedicals

Inhibitors : Ag⁺, Hg²⁺, PCMB; Optimum temperature: 60 to 65 °C; Thermal stability: below 50 °C (pH 6,0; 1 h).

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.

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.

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

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: Abnova

Trichoderma reesei cellulase

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.