You searched for: Enzymes

Supplier: ABNOVA

Recombinant Bovine ENTEROKINASE (from P. pastoris), His-tag

Supplier: MP BIOMEDICALS

Readily soluble in water.

Supplier: MP BIOMEDICALS

Proline specific endopeptidase specifically cleaves peptide bonds on the carboxy side of proline residues.

Supplier: MP BIOMEDICALS

One unit will hydrolyse 1,0 µmole of N-alpha-benzoyl-L-arginine ethyl ester (BAEE) per minute at 25 °C and pH 6,2.

Supplier: MP BIOMEDICALS

Dissolve at a concentration of 1 mg/ml. Dilute further to a concentration of 20 to 60 U/ml immediately before the assay.

Supplier: MP BIOMEDICALS

Neuraminidase of non-pathogenic streptococci, is prepared from the culture filtrate by Ammonium Sulfate precipitation and Ion-exchange chromatography.

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

Zymolyase 100T is used to lyse living yeast cell walls to produce protoplast or spheroplast of various strains of yeast cells. It may also be used for glucan hydrolysis.

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.

Supplier: ABNOVA

Recombinant Poly(A) Polymerase (from E. coli)

Supplier: ABNOVA

Recombinant Alkaline Phosphatase (from E. coli)

Supplier: MP BIOMEDICALS

Diaphorase (from Clostridium kluyveri)

Supplier: ABNOVA

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

Supplier: ABNOVA

Synthetic Yeast Inorganic Pyrophosphatase (from E. coli)

Supplier: MP BIOMEDICALS

Aspergillus niger Type X glucose oxidase

Supplier: MP BIOMEDICALS

Soluble in distilled water or dilute buffer; dissolves readily at 5 mg/ml in 0,1 M potassium phosphate pH 7,4.

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

Preparation Method
Produced from 3× crystallised chymotrypsinogen

α-Chymotrypsin is used for treating pancreatic insufficiency and in traumatology.

Chymotrypsin preferentially catalyses the hydrolysis of peptide bonds involving L-isomers of tyrosine, phenylalanine, and tryptophan. It also readily acts upon amides and esters of susceptible amino acids. In addition to bonds involving aromatic amino acids, chymotrypsin catalyses at a high rate the hydrolysis of bonds of leucyl, methionyl, asparaginyl, and glutamyl residues. a-Chymotrypsin is a protein consisting of 241 amino acid residues. The molecule has three peptide chains: an A chain of 13 residues, a B chain of 131 residues, and a C chain of 97 residues.

Supplier: Merck

Cellulase, enzyme blend contains cellulases, ß-glucosidases, and hemicellulase, for the application of degrading cellulose to fermentable sugars.

Supplier: Merck

The enzyme can be initially dissolved in 50 mM Hepes/KOH pH 7,4, 150 mM NaCl at 10 mg/ml.

Supplier: Merck

Aspergillus oryzae α-amylase enzyme catalyzes the hydrolysis of the α-1,4 glycosidic bonds in soluble starches and related subsrates. These substrates are broken down to release short oligosaccharides and α-limit dextrins. Also act as control enzyme in agar plate-based and carboxymethylcellulose-based clearing assays to screen cellulase activity.

Supplier: Merck

ADH (alcohol dehydrogenase) is a enzymes for biofuel cell research.

Supplier: Merck

Protease is an enzyme used to break down proteins by hydrolysing peptide bonds.

Supplier: Merck

Butyrylcholinesterase from equine serum has been used in a microcalorimetric study of the inhibition of butyrylcholinesterase by paraoxon. This enzyme has also been used in a study to investigate the synthesis and inhibition of cholinergic enzymes.

Supplier: Merck

Ascorbate Oxidase is an enzyme belonging to the family of oxidoreductases that catalyses the reaction: Ascorbic acid + ½ O₂ ascorbate oxidase → Dehydroascorbic acid + H₂O.

Supplier: Merck

SOLu-Trypsin is an advanced proteomics grade enzyme that is solution stable for mass spectrometry. Recombinant, expressed in Pichia pastoris.

Supplier: Merck

The trypsin molecule has two domains: one is related to the enzyme active site and the tryptophan residues; the other is related to the 8-anilinonaphthalene-1-sulfonate binding.

Supplier: Merck

Acetylcholinesterase from Electrophorus electricus is a tetramer composed of 4 equal subunits of 70 kDa each. Each subunit contains one active site. The enzyme is a glycoprotein containing hexosamines.

Supplier: Merck

α-Chymotrypsin is a serine peptidase and has 241 amino acid residues contained in three polypeptide chains (A chain-13 residues, B chain-131 residues, and C chain-97 residues) linked by disulfide bridges. Molecular weight of this enzyme is found to be 25 kDa. Its pI is 8,75. It selectively hydrolyses peptide bonds on the C-terminal side of tyrosine, phenylalanine, tryptophan, and leucine. Ca²⁺ activates and stabilizes the enzyme. The enzyme is inhibited by diisopropyl fluorophosphate (DFP), phenylmethanesulfonyl fluoride (PMSF), N-p-tosyl-L-phenylalanine chloromethyl ketone (TPCK), chymostatin, aprotinin, α1-antitrypsin, α2-macroglobulin, 10 mM Cu²⁺ and Hg²⁺.A serine protease that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains (Tyr, Trp, Phe, Met, Leu) on the carboxyl end of the bond.

Supplier: Merck

Glucose-6-phosphate dehydrogenase is used to test ketose reductase activity in developing maize endosperm. It catalyses the conversion of glucose-6-phosphate to 6-phosphogluconolacetone as the first step in the pentose phosphate pathway. Also it is a key regulatory enzyme in the first step of the pentose phosphate pathway.