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Description: Deoxyribonuclease I gene is approximately 3.2 kb long with 9 exons separated by 8 introns. In the form of a bovine pancreatic enzyme preparation, it occupies an important place in the history of protein chemistry and enzymology: it was the first enzyme to be recognised as specific for DNA; it was the first DNase to be crystallised; and it was the first DNase for which a specific protein inhibitor was characterised. DNase I is a Ca2+ and Mg2+ dependant endonuclease. DNase I is synthesised in the pancreas and stored in zymogen granules. It has been used to reduce the viscosity of cystic fibrosis sputum. A DNase I-like enzyme appears to catalyze the degradation of chromatin to oligo- and mononucleosomes during apoptosis. A recent study has demonstrated an endonuclease with activity and antigenicity indistinguishable from DNase I in thymocytes, cells susceptible to apoptosis. DNase I is an endonuclease that hydrolyzes double-stranded or single stranded DNA preferentially at sites adjacent to pyrimidine nucleotides. The product of hydrolysis is a complex mixture of 5'-phosphate mononucleotides and oligonucleotides. In the presence of Mg ion, DNase I attacks each strand of DNA independently and the cleavage sites are random.
Numéro de catalogue: BOSSBS-7651R-A750
UOM: 1 * 100 µl
Fournisseur: Bioss


Description: Deoxyribonuclease I gene is approximately 3.2 kb long with 9 exons separated by 8 introns. In the form of a bovine pancreatic enzyme preparation, it occupies an important place in the history of protein chemistry and enzymology: it was the first enzyme to be recognized as specific for DNA; it was the first DNase to be crystallized; and it was the first DNase for which a specific protein inhibitor was characterized. DNase I is a Ca2+ and Mg2+ dependant endonuclease. DNase I is synthesized in the pancreas and stored in zymogen granules. It has been used to reduce the viscosity of cystic fibrosis sputum. A DNase I-like enzyme appears to catalyze the degradation of chromatin to oligo- and mononucleosomes during apoptosis. A recent study has demonstrated an endonuclease with activity and antigenicity indistinguishable from DNase I in thymocytes, cells susceptible to apoptosis. DNase I is an endonuclease that hydrolyzes double-stranded or single stranded DNA preferentially at sites adjacent to pyrimidine nucleotides. The product of hydrolysis is a complex mixture of 5'-phosphate mononucleotides and oligonucleotides. In the presence of Mg ion, DNase I attacks each strand of DNA independently and the cleavage sites are random.
Numéro de catalogue: BOSSBS-7651R-A488
UOM: 1 * 100 µl
Fournisseur: Bioss


Description: Below 35 to 40 °C gelatin swells and absorbs approximately 5 to 10 times its weight of water to form a gel. Gelatin is soluble in glycerol and acetic acid, and more soluble in hot than in cold water. It is practically insoluble in most organic solvents such as alcohol, chloroform, carbon disulphide, carbon tetrachloride, ether, benzene, acetone and oils. Sterile solutions of gelatin stored cold are stable indefinitely, but at elevated temperatures hydrolysis or rupture of peptide bonds occurs, increasing the number of free amino groups. Gel strength and viscosity gradually weaken upon prolonged heating in solution above ~40 °C; this degradation is accelerated by extremes in pH, proteolytic enzymes and bacterial action.
Numéro de catalogue: ICNA0296031790
UOM: 1 * 500 g
Fournisseur: MP Biomedicals


Description: Deoxyribonuclease I gene is approximately 3.2 kb long with 9 exons separated by 8 introns. In the form of a bovine pancreatic enzyme preparation, it occupies an important place in the history of protein chemistry and enzymology: it was the first enzyme to be recognized as specific for DNA; it was the first DNase to be crystallized; and it was the first DNase for which a specific protein inhibitor was characterized. DNase I is a Ca2+ and Mg2+ dependant endonuclease. DNase I is synthesized in the pancreas and stored in zymogen granules. It has been used to reduce the viscosity of cystic fibrosis sputum. A DNase I-like enzyme appears to catalyze the degradation of chromatin to oligo- and mononucleosomes during apoptosis. A recent study has demonstrated an endonuclease with activity and antigenicity indistinguishable from DNase I in thymocytes, cells susceptible to apoptosis. DNase I is an endonuclease that hydrolyzes double-stranded or single stranded DNA preferentially at sites adjacent to pyrimidine nucleotides. The product of hydrolysis is a complex mixture of 5'-phosphate mononucleotides and oligonucleotides. In the presence of Mg ion, DNase I attacks each strand of DNA independently and the cleavage sites are random.
Numéro de catalogue: BOSSBS-7651R
UOM: 1 * 100 µl
Fournisseur: Bioss


Description: Deoxyribonuclease I gene is approximately 3.2 kb long with 9 exons separated by 8 introns. In the form of a bovine pancreatic enzyme preparation, it occupies an important place in the history of protein chemistry and enzymology: it was the first enzyme to be recognized as specific for DNA; it was the first DNase to be crystallized; and it was the first DNase for which a specific protein inhibitor was characterized. DNase I is a Ca2+ and Mg2+ dependant endonuclease. DNase I is synthesized in the pancreas and stored in zymogen granules. It has been used to reduce the viscosity of cystic fibrosis sputum. A DNase I-like enzyme appears to catalyze the degradation of chromatin to oligo- and mononucleosomes during apoptosis. A recent study has demonstrated an endonuclease with activity and antigenicity indistinguishable from DNase I in thymocytes, cells susceptible to apoptosis. DNase I is an endonuclease that hydrolyzes double-stranded or single stranded DNA preferentially at sites adjacent to pyrimidine nucleotides. The product of hydrolysis is a complex mixture of 5'-phosphate mononucleotides and oligonucleotides. In the presence of Mg ion, DNase I attacks each strand of DNA independently and the cleavage sites are random.
Numéro de catalogue: BOSSBS-7651R-CY5
UOM: 1 * 100 µl
Fournisseur: Bioss


Description: Deoxyribonuclease I gene is approximately 3.2 kb long with 9 exons separated by 8 introns. In the form of a bovine pancreatic enzyme preparation, it occupies an important place in the history of protein chemistry and enzymology: it was the first enzyme to be recognized as specific for DNA; it was the first DNase to be crystallized; and it was the first DNase for which a specific protein inhibitor was characterized. DNase I is a Ca2+ and Mg2+ dependant endonuclease. DNase I is synthesized in the pancreas and stored in zymogen granules. It has been used to reduce the viscosity of cystic fibrosis sputum. A DNase I-like enzyme appears to catalyze the degradation of chromatin to oligo- and mononucleosomes during apoptosis. A recent study has demonstrated an endonuclease with activity and antigenicity indistinguishable from DNase I in thymocytes, cells susceptible to apoptosis. DNase I is an endonuclease that hydrolyzes double-stranded or single stranded DNA preferentially at sites adjacent to pyrimidine nucleotides. The product of hydrolysis is a complex mixture of 5'-phosphate mononucleotides and oligonucleotides. In the presence of Mg ion, DNase I attacks each strand of DNA independently and the cleavage sites are random.
Numéro de catalogue: BOSSBS-7651R-CY5.5
UOM: 1 * 100 µl
Fournisseur: Bioss


Description: Deoxyribonuclease I gene is approximately 3.2 kb long with 9 exons separated by 8 introns. In the form of a bovine pancreatic enzyme preparation, it occupies an important place in the history of protein chemistry and enzymology: it was the first enzyme to be recognized as specific for DNA; it was the first DNase to be crystallized; and it was the first DNase for which a specific protein inhibitor was characterized. DNase I is a Ca2+ and Mg2+ dependant endonuclease. DNase I is synthesized in the pancreas and stored in zymogen granules. It has been used to reduce the viscosity of cystic fibrosis sputum. A DNase I-like enzyme appears to catalyze the degradation of chromatin to oligo- and mononucleosomes during apoptosis. A recent study has demonstrated an endonuclease with activity and antigenicity indistinguishable from DNase I in thymocytes, cells susceptible to apoptosis. DNase I is an endonuclease that hydrolyzes double-stranded or single stranded DNA preferentially at sites adjacent to pyrimidine nucleotides. The product of hydrolysis is a complex mixture of 5'-phosphate mononucleotides and oligonucleotides. In the presence of Mg ion, DNase I attacks each strand of DNA independently and the cleavage sites are random.
Numéro de catalogue: BOSSBS-7651R-FITC
UOM: 1 * 100 µl
Fournisseur: Bioss


Description: Deoxyribonuclease I gene is approximately 3.2 kb long with 9 exons separated by 8 introns. In the form of a bovine pancreatic enzyme preparation, it occupies an important place in the history of protein chemistry and enzymology: it was the first enzyme to be recognized as specific for DNA; it was the first DNase to be crystallized; and it was the first DNase for which a specific protein inhibitor was characterized. DNase I is a Ca2+ and Mg2+ dependant endonuclease. DNase I is synthesized in the pancreas and stored in zymogen granules. It has been used to reduce the viscosity of cystic fibrosis sputum. A DNase I-like enzyme appears to catalyze the degradation of chromatin to oligo- and mononucleosomes during apoptosis. A recent study has demonstrated an endonuclease with activity and antigenicity indistinguishable from DNase I in thymocytes, cells susceptible to apoptosis. DNase I is an endonuclease that hydrolyzes double-stranded or single stranded DNA preferentially at sites adjacent to pyrimidine nucleotides. The product of hydrolysis is a complex mixture of 5'-phosphate mononucleotides and oligonucleotides. In the presence of Mg ion, DNase I attacks each strand of DNA independently and the cleavage sites are random.
Numéro de catalogue: BOSSBS-7651R-A350
UOM: 1 * 100 µl
Fournisseur: Bioss


Description: Deoxyribonuclease I gene is approximately 3.2 kb long with 9 exons separated by 8 introns. In the form of a bovine pancreatic enzyme preparation, it occupies an important place in the history of protein chemistry and enzymology: it was the first enzyme to be recognized as specific for DNA; it was the first DNase to be crystallized; and it was the first DNase for which a specific protein inhibitor was characterized. DNase I is a Ca2+ and Mg2+ dependant endonuclease. DNase I is synthesized in the pancreas and stored in zymogen granules. It has been used to reduce the viscosity of cystic fibrosis sputum. A DNase I-like enzyme appears to catalyze the degradation of chromatin to oligo- and mononucleosomes during apoptosis. A recent study has demonstrated an endonuclease with activity and antigenicity indistinguishable from DNase I in thymocytes, cells susceptible to apoptosis. DNase I is an endonuclease that hydrolyzes double-stranded or single stranded DNA preferentially at sites adjacent to pyrimidine nucleotides. The product of hydrolysis is a complex mixture of 5'-phosphate mononucleotides and oligonucleotides. In the presence of Mg ion, DNase I attacks each strand of DNA independently and the cleavage sites are random.
Numéro de catalogue: BOSSBS-7651R-A647
UOM: 1 * 100 µl
Fournisseur: Bioss


Description: Use of dextrans as long and hydrophilic spacer arms improves the performance of immobilized proteins acting on macromolecules. Dextrans are used in many applications as platelet aggregants, plasma volume extenders, osmotic pressure regulators, stabilizers, organ separation media, matrix components, copolymers, microcarriers, binding agents, viscosity modifiers, antithrombotics, lubricants and physical structure components. They may be used as long hydrophilic spacer arms to improve the performance (freedom of movement) of conjugated/bound proteins. Dextrans may be derivatized for use in biosensor systems.

Dextran is branched polysaccharide made up of linear α (1→6) linked glucose units and α (1→3) link initiated branches; it ranges in size from 10,000 to 150,000 Kd.Depending upon its molecular weight it has different uses in different fields.
Numéro de catalogue: ICNA0218014050
UOM: 1 * 50 g
Fournisseur: MP Biomedicals


Description: Deoxyribonuclease I gene is approximately 3.2 kb long with 9 exons separated by 8 introns. In the form of a bovine pancreatic enzyme preparation, it occupies an important place in the history of protein chemistry and enzymology: it was the first enzyme to be recognized as specific for DNA; it was the first DNase to be crystallized; and it was the first DNase for which a specific protein inhibitor was characterized. DNase I is a Ca2+ and Mg2+ dependant endonuclease. DNase I is synthesized in the pancreas and stored in zymogen granules. It has been used to reduce the viscosity of cystic fibrosis sputum. A DNase I-like enzyme appears to catalyze the degradation of chromatin to oligo- and mononucleosomes during apoptosis. A recent study has demonstrated an endonuclease with activity and antigenicity indistinguishable from DNase I in thymocytes, cells susceptible to apoptosis. DNase I is an endonuclease that hydrolyzes double-stranded or single stranded DNA preferentially at sites adjacent to pyrimidine nucleotides. The product of hydrolysis is a complex mixture of 5'-phosphate mononucleotides and oligonucleotides. In the presence of Mg ion, DNase I attacks each strand of DNA independently and the cleavage sites are random.
Numéro de catalogue: BOSSBS-7651R-CY7
UOM: 1 * 100 µl
Fournisseur: Bioss


Description: Deoxyribonuclease I gene is approximately 3.2 kb long with 9 exons separated by 8 introns. In the form of a bovine pancreatic enzyme preparation, it occupies an important place in the history of protein chemistry and enzymology: it was the first enzyme to be recognized as specific for DNA; it was the first DNase to be crystallized; and it was the first DNase for which a specific protein inhibitor was characterized. DNase I is a Ca2+ and Mg2+ dependant endonuclease. DNase I is synthesized in the pancreas and stored in zymogen granules. It has been used to reduce the viscosity of cystic fibrosis sputum. A DNase I-like enzyme appears to catalyze the degradation of chromatin to oligo- and mononucleosomes during apoptosis. A recent study has demonstrated an endonuclease with activity and antigenicity indistinguishable from DNase I in thymocytes, cells susceptible to apoptosis. DNase I is an endonuclease that hydrolyzes double-stranded or single stranded DNA preferentially at sites adjacent to pyrimidine nucleotides. The product of hydrolysis is a complex mixture of 5'-phosphate mononucleotides and oligonucleotides. In the presence of Mg ion, DNase I attacks each strand of DNA independently and the cleavage sites are random.
Numéro de catalogue: BOSSBS-7651R-CY3
UOM: 1 * 100 µl
Fournisseur: Bioss


Description: Deoxyribonuclease I gene is approximately 3.2 kb long with 9 exons separated by 8 introns. In the form of a bovine pancreatic enzyme preparation, it occupies an important place in the history of protein chemistry and enzymology: it was the first enzyme to be recognized as specific for DNA; it was the first DNase to be crystallized; and it was the first DNase for which a specific protein inhibitor was characterized. DNase I is a Ca2+ and Mg2+ dependant endonuclease. DNase I is synthesized in the pancreas and stored in zymogen granules. It has been used to reduce the viscosity of cystic fibrosis sputum. A DNase I-like enzyme appears to catalyze the degradation of chromatin to oligo- and mononucleosomes during apoptosis. A recent study has demonstrated an endonuclease with activity and antigenicity indistinguishable from DNase I in thymocytes, cells susceptible to apoptosis. DNase I is an endonuclease that hydrolyzes double-stranded or single stranded DNA preferentially at sites adjacent to pyrimidine nucleotides. The product of hydrolysis is a complex mixture of 5'-phosphate mononucleotides and oligonucleotides. In the presence of Mg ion, DNase I attacks each strand of DNA independently and the cleavage sites are random.
Numéro de catalogue: BOSSBS-7651R-HRP
UOM: 1 * 100 µl
Fournisseur: Bioss


Description: Deoxyribonuclease I gene is approximately 3.2 kb long with 9 exons separated by 8 introns. In the form of a bovine pancreatic enzyme preparation, it occupies an important place in the history of protein chemistry and enzymology: it was the first enzyme to be recognised as specific for DNA; it was the first DNase to be crystallised; and it was the first DNase for which a specific protein inhibitor was characterised. DNase I is a Ca2+ and Mg2+ dependant endonuclease. DNase I is synthesised in the pancreas and stored in zymogen granules. It has been used to reduce the viscosity of cystic fibrosis sputum. A DNase I-like enzyme appears to catalyze the degradation of chromatin to oligo- and mononucleosomes during apoptosis. A recent study has demonstrated an endonuclease with activity and antigenicity indistinguishable from DNase I in thymocytes, cells susceptible to apoptosis. DNase I is an endonuclease that hydrolyzes double-stranded or single stranded DNA preferentially at sites adjacent to pyrimidine nucleotides. The product of hydrolysis is a complex mixture of 5'-phosphate mononucleotides and oligonucleotides. In the presence of Mg ion, DNase I attacks each strand of DNA independently and the cleavage sites are random.
Numéro de catalogue: BOSSBS-7651R-A680
UOM: 1 * 100 µl
Fournisseur: Bioss


Description: Deoxyribonuclease I gene is approximately 3.2 kb long with 9 exons separated by 8 introns. In the form of a bovine pancreatic enzyme preparation, it occupies an important place in the history of protein chemistry and enzymology: it was the first enzyme to be recognized as specific for DNA; it was the first DNase to be crystallized; and it was the first DNase for which a specific protein inhibitor was characterized. DNase I is a Ca2+ and Mg2+ dependant endonuclease. DNase I is synthesized in the pancreas and stored in zymogen granules. It has been used to reduce the viscosity of cystic fibrosis sputum. A DNase I-like enzyme appears to catalyze the degradation of chromatin to oligo- and mononucleosomes during apoptosis. A recent study has demonstrated an endonuclease with activity and antigenicity indistinguishable from DNase I in thymocytes, cells susceptible to apoptosis. DNase I is an endonuclease that hydrolyzes double-stranded or single stranded DNA preferentially at sites adjacent to pyrimidine nucleotides. The product of hydrolysis is a complex mixture of 5'-phosphate mononucleotides and oligonucleotides. In the presence of Mg ion, DNase I attacks each strand of DNA independently and the cleavage sites are random.
Numéro de catalogue: BOSSBS-7651R-A555
UOM: 1 * 100 µl
Fournisseur: Bioss


Description: VISCOSITY STANDARD N.4 1 * 500 mL
Numéro de catalogue: REGEREVIS-N.4
UOM: 1 * 500 mL
Fournisseur: REAGECON