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Restriction enzymes, modifying enzymes, buffering solutions, inhibitors, and substrates for use in clinical, research, and general laboratory procedures.
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Bacteroides Heparinase II (also called Heparin Lyase II) is cloned from Bacteroides eggerthii. It is a low specificity enzyme that is active on both heparin and heparan sulfate. Bacteroides Heparinase II cleaves the glycosidic bond between N-sulfated and glucuronic or iduronic acid residues. The reaction yields oligosaccharide products containing unsaturated uronic acids which can be detected by UV spectroscopy at 232 nm. When used alone this enzyme rarely yields complete depolymerization of a polysaccharide chain, however disaccharide analysis is enhanced when used in combination with Heparinase I and III.
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Bacteroides Heparinase III, also called Heparin Lyase III, is active on both heparin and heparan sulfate. Bacteroides Heparinase III can cleave the glycosidic bond between hexosamines and either iduronic acid or glucuronic acid residues. It is active in the presence of 6-sulfation. The reaction yields oligosaccharide products containing unsaturated uronic acids, which can be detected by UV spectroscopy at 232 nm
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A salt tolerant variant of T4 DNA Ligase, Salt-T4 DNA Ligase catalyzes the formation of a phosphodiester bond between juxtaposed 5 phosphate and 3 hydroxyl termini in duplex DNA or RNA and is designed to function at higher salt concentrations than wild type T4 DNA Ligase. This enzyme will join cohesive end termini at salt concentrations as high as 300 mM without any loss in activity. This enzyme is insensitive to salt carried over from other reaction components (vector or insert DNA) and allows ligation reactions to proceed in alternative reaction buffers with higher levels of salt (e.g., NEBuffer r3.1).
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Alternative name: Histone deacetylase 1. Formulation: Liquid. In 50mM TRIS, pH 8.0, 138mM sodium chloride and 10% glycerol. Source: Produced in insect cells. HDAC1 from human cDNA (482 aa). Produced in a baculovirus expression system. Long Term Storage: -80°C.
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Activation of Prekallikrein with Factor alpha -XIIa produces the enzymatically active Kallikrein. Kallikrein is a serine protease which consists of a heavy chain (Mr 52kD) and light chains (Mr either 36 or 33 kD) linked by disulfide bridges.
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