Enzymes

Alkaline phosphatase is an enzyme commonly used for the removal of terminal phosphates from the 5' end of DNA or RNA strands to prevent reannealing of the cohesive ends and facilitate future radiolabeling of the strands.

This system includes 30 U/μL of alkaline phosphatase in a 50% glycerol solution and a dilution buffer that allows for the preparation of a 3 U/μL solution for use in DNA modification.

Cellulase R-10, also called Cellulase "Onozuka" R-10, is derived from Trichoderma Viride. Cellulase R-10 is a multi-enzymatic system consisting of various enzymes, including cellulase, hemicellulase, pectinase and protease. Cellulase R-10 is typically used in association with macerozyme R-10 in the decomposition of plant cell walls to produce protoplasts.

Cellulase “Onozuka RS” is produced by a mutant Trichoderma viride that was derived from the parent strain for Cellulase “Onozuka -R-10”. Cellulase RS contains a very high activity of decomposing natural celluloses. This type of cellulase can be used to obtain protoplasts in a very short time and dissolves cell walls of a wider range of plants.

DNase I (Deoxyribonuclease I) is a dialyzed lyophilized powder from bovine pancreas that has been purified by chromatography.

Bovine pancreatic deoxyribonuclease (DNase) is an endonuclease, which splits phosphodiester linkages preferentially adjacent to a pyrimidine nucleotide yielding polynucleotides with a free hydroxyl group at the 3' position and a phosphate group at the 5' position. The optimum pH is 7.8.

DNase I is activated by bivalent metals and inhibited by chelating agents such as EDTA and SDS. DNase I can be stabilized against proteolytic digestion by 5mM Ca2+.

DNase I (Deoxyribonuclease I) is a dialyzed lyophilized powder from bovine pancreas that has been purified by chromatography.

Bovine pancreatic deoxyribonuclease (DNase) is an endonuclease which splits phosphodiester linkages, preferentially adjacent to a pyrimidine nucleotide yielding polynucleotides with a free hydroxyl group at the 3' position and phosphate group at the 5' position. The optimum pH is 7.8.

DNase I is activated by bivalent metals, and inhibited by chelating agents such as EDTA and SDS. DNase I can be stabilized against proteolytic digestion by 5mM Ca 2+.

DNase I (Deoxyribonuclease I) is a dialyzed lyophilized powder from bovine pancreas that has been purified by chromatography.

Bovine pancreatic deoxyribonuclease (DNase) is an endonuclease which splits phosphodiester linkages, preferentially adjacent to a pyrimidine nucleotide yielding polynucleotides with a free hydroxyl group at the 3' position and phosphate group at the 5' position. The optimum pH is 7.8.

DNase I is activated by bivalent metals, and inhibited by chelating agents such as EDTA and SDS. DNase I can be stabilized against proteolytic digestion by 5 mM Ca²⁺.

Elastase is used for tissue dissociation and cell isolation applications. Elastase has an activity of >30 units/mg and is unstable at < pH 3.5. Elastase was purified from a porcine pancreas and then purified by affinity chromatography to remove trace amounts of contaminating proteases. One unit corresponds to the amount of enzyme which liberates 1 µmol 4-nitroaniline per minute at 25°C and pH 7.8.

Glucose oxidase comes from Aspergillus niger and has many applications. Glucose oxidase can be used in the determination of glucose in colorimetric assays in conjunction with peroxidase, in the determination of glucose biosensors or for use as an enzyme label.

Glucose oxidase comes from Aspergillus niger and has many applications. Glucose oxidase can be used in the determination of glucose in colorimetric assays in conjunction with peroxidase, in the determination of glucose biosensors or for use as en enzyme label.

Horseradish peroxidase (HRP) is the most commonly used antibody-conjugated enzyme. Substrates for HRP are luminol and benzidine substrates. Tetramethylbenzidine (TMB) and similar substrates are oxidized by HRP in the presence of hydrogen peroxide, or nontoxic substitutes, to yield a chinoid structure of intense blue color.

Lysozyme is an enzyme capable of breaking down the bacterial cell wall, and is typically used to enhance protein extractions or nucleic acid extractions. It works by hydrolyzing the 1,4-β-linkages located between the N-acetylmuramic acid and the N-acetyl-D-glucosamine residues in peptidoglycan.

Gram-positive cells have an increased susceptibility to the actions of lysozyme since gram-positive cells have a higher quantity of peptidoglycan in the cell wall. Gram-negative cells are less vulnerable, but can still be hydrolyzed in the presence of EDTA.

Macerozyme R-10 is a macerating enzyme from the Rhizopus sp. which is perfectly suited for the isolation of plant cells. Macerozyme R-10 is often used in combination with Cellulase "Onozuka R-10" in the isolation of plant protoplasts.

Proteinase K is a highly reactive nonspecific serine protease that belongs to the subtilisin family of proteins. It cleaves at the carboxylic acid side of aliphatic, aromatic, or hydrophobic amino acids. Proteinase K is capable of inactivating RNases and DNases and is used in the isolation or preparation of high molecular weight nucleic acids. Proteinase K is also useful for helping to characterize enzymes, due to its cleavage specificity. This enzyme was designated proteinase K because of its ability to hydrolyze keratin. Proteinase K is stable in a wide variety of detergents and buffer salts and at various temperatures and pH. The isoelectric point of proteinase K is 8.9.

Proteinase K is a highly reactive nonspecific serine protease that belongs to the subtilisin family of proteins. It cleaves at the carboxylic acid side of aliphatic, aromatic, or hydrophobic amino acids. Proteinase K is capable of inactivating RNases and DNases and is used in the isolation or preparation of high molecular weight nucleic acids. Proteinase K is also useful for helping to characterize enzymes, due to its cleavage specificity. This enzyme was designated proteinase K because of its ability to hydrolyze keratin. Proteinase K is stable in a wide variety of detergents and buffer salts and at various temperatures and pH. The isoelectric point of proteinase K is 8.9.

RNase A, isolated from bovine pancreas, degrades single-stranded RNA at the C and U residues; therefore, RNase A is pyrimidine specific. Degradation occurs by cleaving the phosphodiester bond located between the 5’-ribose of the nucleotide and the phosphate group that is connected to the 3’-ribose of the neighboring pyrimidine.

Trypsin is a serine protease found in the digestive system of many vertebrates where it hydrolyzes proteins. Through trypsinisation, it cleaves peptides at the carboxyl side of arginine and lysine, unless they are followed by a proline.

Trypsin has an optimal operating pH of about 7.5-8.5 and optimal operating temperature of about 37°C. Unlike chymotrypsin, the activity of trypsin is not affected by the inhibitor tosyl phenylalanyl chloromethyl ketone (TPCK).

Trypsin is a serine protease found in the digestive system of many vertebrates where it hydrolyzes proteins. Through trypsinisation, it cleaves peptides at the carboxyl side of arginine and lysine, unless they are followed by a proline.

Trypsin has an optimal operating pH of about 7.5-8.5 and optimal operating temperature of about 37°C. Unlike chymotrypsin, the activity of trypsin is not affected by the inhibitor tosyl phenylalanyl chloromethyl ketone (TPCK).

Trypsin 1:300 indicates that one part trypsin will digest 300 parts casein in the USP activity assay.

Trypsin is a serine protease found in the digestive system of many vertebrates where it hydrolyzes proteins. Through trypsinisation, it cleaves peptides at the carboxyl side of arginine and lysine, unless they are followed by a proline.

Trypsin has an optimal operating pH of about 7.5-8.5 and optimal operating temperature of about 37°C. Unlike chymotrypsin, the activity of trypsin is not affected by the inhibitor tosyl phenylalanyl chloromethyl ketone (TPCK).