Supplier: Merck

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

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

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

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

Chymotrypsin (Chy) is a serine protease. It corresponds to a molecular weight of 25,7 kDa and is widely used in pharmaceutical industry.It is synthesized in pancreas from chymotrypsinogen and require calcium for this conversion.α-Chymotrypsin from bovine pancreas (bovine pancreatic α-chymotrypsin, CHT) is an enzyme protein.The influence of varying concentrations of organic solvents like ethanol, 1,4-dioxane and acetonitrile on CHT has been reported.

Supplier: Merck

A mixture of at least three proteolytic activities including an extracellular serine protease. In general, serine proteases display a wide range of substrate specificities, which are believed to be mediated by an active site composed of one Asp, one His, and a Ser residue in the molecule. This enzyme prefers to hydrolyze peptide bonds on the carboxyl side of glutamic or aspartic acid.

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.

Supplier: Merck

Horseradish peroxidase, Typ I

Supplier: Merck

L-Lactate dehydrogenase Typ II (from Muscle)

Supplier: Merck

Ribonuclease A, type XII-A, from bovine pancreas.

Supplier: Merck

Xanthine oxidase from bovine milk, Grade I.

Supplier: Merck

Lysozyme is abundantly found in animal and plant kingdoms. It is a natural food preservative and also found to be present in specific bacterial cell walls. Lysozyme is usually present in tears, milk, urine and saliva.Enzyme breaks down the cell walls of bacteria; used to prepare spheroplasts.

Supplier: Merck

Trichoderma viride cellulase

Supplier: Merck

Horseradish peroxidase, Typ II

Supplier: Merck

Human alpha-chymotrypsin (from Pancreas)

Supplier: Merck

Pig L-Lactate dehydrogenase (from Heart)

Supplier: Merck

Bovine L-lactate dehydrogenase Typ X (from Muscle)

Supplier: Merck

Bovine alpha-Chymotrypsin type I-S (from Pancreas)

Supplier: Merck

Xanthine oxidase from Buttermilk, grade III.

Supplier: Merck

Bovine alpha-Chymotrypsin type II (from Pancreas)

Supplier: Merck

Lysozyme hydrolyzes β(1→4) linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrin. Gram-positive cells are quite susceptible to this hydrolysis as their cell walls have a high proportion of peptidoglycan. Gram-negative bacteria are less susceptible due to the presence of an outer membrane and a lower proportion of peptidoglycan. However, these cells may be hydrolyzed in the presence of EDTA that chelates metal ions in the outer bacterial membrane.The enzyme is active over a broad pH range (6,0 to 9,0). At pH 6,2, maximal activity is observed over a wider range of ionic strengths (0,02 to 0,100 M) than at pH 9,2 (0,01 to 0,06 M).

Supplier: Merck

Alcohol oxidase is from Pichia pastoris used to study protein translocation into peroxisomes. Also used for the bacterial expression and immunological verification of Hv-p68 cDNA clones.

Supplier: Merck

Pepsin

Supplier: Merck

Horseradish peroxidase

Supplier: Merck

Desoxyribonuclease II

Supplier: Merck

Invertase glycoprotein standard.

Supplier: Merck

Catalase (from Corynebacterium glutamicum)

Supplier: Merck

Pig Pancreatin (from Pancreas)

Supplier: Merck

Xanthine oxidase (from buttermilk)

Supplier: Merck

Horseradish peroxidase, Typ XII