Properties
Description
Recombinant Streptococcus pneumoniae sialidase 33A2 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
Streptococcus pneumoniae
Purity
≥90%, determined by SDS-PAGE.
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 Streptococcus pneumoniae sialidase 33A2 can be used in clinical chemistry, glycobiology, and carbohydrate research. It has the ability to hydrolyze glycoprotein human alpha-1 (AGP), and sialic acids.
