Sialidase Sp cleaves the non-reducing terminal α(2-3) unbranched sialic acid residues from complex carbohydrates and glycoproteins.
recombinant from Streptococcus pneumoniae in E. Coli
Part Number – Amount of Enzyme
E-S007 – 60 µLs¹
E-S007-20 – 20 µLs¹
E-S007-200 – 200 µls²
¹ includes buffer
² includes enzyme only
$198 – $1,377
Sialidase, N-acetylneuraminate glycohydrolase, Exo-alpha-sialidase
α(2-3) Neuraminidase Sp cleaves exclusively the non-reducing terminal α(2-3) unbranched sialic acid residues from complex carbohydrates and glycoproteins. There is no detectable activity on α(2-6) or α(2-8) linkages or on branched α(2-3) linkages . To cleave all non-reducing terminal sialic acid residues including branched sialic acids (linked to an internal residue) from complex carbohydrates and glycoproteins, use α(2-3,6,8,9) Neuraminidase Au (E-S001).
Source recombinant Streptococcus pneumoniae in E. Coli
Neuraminidase Sp in 50 mM sodium phosphate, pH 7.5
Included with 20 µL and 60 µL pack sizes:
5x Reaction Buffer 250 mM sodium phosphate, pH 6.0
Specific Activity ≥ 250 U/mg
Activity ≥ 10 U/ml
Molecular weight~75,000 daltons
pH optimum 6.0
Suggested usage 1. Add up to 100 μg of glycoprotein or 1 nmol of oligosaccharide to tube.
2. Add water to 14 μL
3. Add 4 μL 5X Reaction Buffer.
4. Add 2 μL α (2-3) Neuraminidase.
5. Incubate at 37°C for 1 hour
Desialylation may be monitored by SDS-PAGE if the size differential between native and desialylated protein is sufficient for detection.
Specifictity Cleaves the non-reducing terminal alpha-(2-3) unbranched sialic acid residues from complex carbohydrates and glycoproteins.
Specific Activity Defined as the amount of enzyme required to produce 1 µmole of methylumbelliferone in 1 minute at 37˚C, pH 5.0 from MU-NANA [2′-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid].
Storage Store enzyme at 4˚C.
Neuraminidase Sp References
Corfield, A. P., H. Higa, J. C. Paulson and R. Schauer. The specificity of viral and bacterial sialidases for alpha(2-3) and alpha(2-6)-linked sialic acids in glycoproteins. Biochim Biophys Acta 744: 121-12 6 (1983).
Dwek, R. A., C. J. Edge, D. J. Harvey, M. R. Wormald and R. B. Parekh. Analysis of glycoprotein-associated oligosaccharides. Ann Rev Biochem 62: 65-100 (1993).
Kobata, A. Use of endo- and exoglycosidases for structural studies of glycoconjugates. Anal Biochem 100: 1-14 (1979).
Glasgow, L R., J. C . Paulson and R. L. Hill. Systematic purification of five glycosidases from Streptococcus pneumoniae. J. Biol Chem 252: 8615-8623 (1977).
Kelly, R. T., D. Greiff and S. Farmer. Neuraminidase activity in Diplococcus pneumoniae. J Bacteriol 91: 601-3 (1965).
Prime, S., J. Dearnley , A. M. Venton, R. B. Parekh and C. J. Edge. Oligosaccharide sequencing based on exo- and endoglycosidase digestion and liquid chromatographic analysis of the products. J Chromatogr A 720: 263-274 (1996).