Recombinant Clostridium perfringens sialidase 33B produced by Escherichia coli, is responsible for hydrolyzing terminal N- or O-acetylneuraminic acids which are α2,3-, α2,6-, α2,8- linked to oligosaccharides, polysaccharides, mucopolysaccharides, glycoproteins, and glycolipids.
Expression System
Escherichia coli
Species
Clostridium perfringens
Concentration
0.25 mg/mL
Form
Liquid
Purity
≥90%, determined by SDS-PAGE.
Activity
Sialidases
Buffer
35 mM NaHepes buffer (pH 7.5), 750 mM NaCl, 200 mM imidazole, 3.5 mM CaCl2, and 25% (v/v) glycerol
Applications
Recombinant Clostridium perfringens sialidase 33B can be used in clinical chemistry, glycobiology, and carbohydrate research. It has the ability to hydrolyze 4-methylumbelliferyl-N-acetyl neuraminic acid, colominic acid, glycolipids, glycoproteins, sialic acids, synthetic substrates.
Publications
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Publications
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