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Sialidase Au
Alpha-(2-3,6,8,9)

recombinant from A. ureafaciens

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Part Number: E-S001

$433.00

Neuraminidase, N-acetylneuraminate glycohydrolase

Part number E-S001
Source recombinant from Arthrobacter ureafaciens in E. Coli.
EC 3.2.1.18

Contents
60 µl aliquot of enzyme (300 mU) in 20 mM Tris-HCl, 25 mM NaCl, pH 7.5
5x Reaction Buffer 250 mM sodium phosphate, pH 6.0

Specific Activity >135 U/mg
Activity 5 U/ml

Molecular weight ~69,000 daltons
pH range 4.5-7, optimum 6.0

Suggested usage
add 2 µL of enzyme to 100 µg of glycoprotein or 1 nmol of oligosaccharide. Add buffer and incubate 3 hours at 37˚C. NOTE: longer incubation times are necessary if branched sialic acids are present.

Specifictity Cleaves all non-reducing terminal branched and unbranched sialic acids

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.

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).

Ohta, Y., Y. Tsukada and T. Sugimori. Purification and properties of neuraminidase isoenzymes in Arthrobacter ureafaciens mutant. J Biochem (Tokyo) 106: 1086- 1089 (1989).

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).

Uchida, Y., Y. Tsukada and T. Sugimori. Enzymatic properties of neuraminidases from Arthrobacter ureafaciens. J Biochem (Tokyo) 86: 573-58 5 (1979).

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