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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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Thermostable 5' App DNA/RNA Ligase is a point mutant of catalytic lysine of RNA ligase from Methanobacterium thermoautotrophicum. This enzyme is ATP independent. It requires a 5' pre-adenylated linker for ligation to the 3' -OH end of either RNA or single stranded DNA (ssDNA). The enzyme is also active in ligation of RNA with 2' -O-methylated 3 end to 5-adenylated linkers. The optimal temperature for ligation reaction is 60-65°C. The mutant ligase is unable to adenylate the 5' -phosphate of RNA or ssDNA, which reduces the formation of undesired ligation products (concatemers and circles). The ability of the ligase to function at 65°C might reduce the constraints of RNA secondary structure in RNA ligation experiments.
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Neuraminidase from Clostridium perfringens (C. welchii) Suitable for manufacturing of diagnostic kits and reagents, Type V, lyophilized powder | 9001-67-6 | MFCD00131711 | 6UN
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Bacteroides Heparinase I, also called Heparin Lyase I, is active on heparin and the highly sulfated domains of heparan sulfate. The reaction yields oligosaccharide products containing unsaturated uronic acids which can be detected by UV spectroscopy at 232 nm.
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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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