N-Acetylneuraminyl Hydrolase
Sialidase

Liquid. In 20 mM Tris-HCl, 20 mM NaCl, pH 7.5. DO NOT FREEZE. Recombinant, Arthrobacter ureafaciens a2-3,6,8,9-Neuraminidase expressed in E. coli. Catalyzes the hydrolysis of all non-reducing terminal sialic acid residues from complex carbohydrates and glycoproteins. High concentrations of this sialidase and prolonged periods of incubation result in the additional cleavage of branched sialic acids. This enzyme is found as two active species of MW 60000 and 69000. Activity: ≥5 units/ml. Specific activity: ≥40 units/mg protein. One unit is defined as the amount of enzyme that will catalyze the release of 1 µmol of methylumbelliferone from 2′-(4-methylumbelliferyl)-a-D-N-acetylneuraminic acid per min at 37°C, pH 5.0. (Note: 1 mU = 1 milliunit). Contaminants: N-acetylglucosaminidase, a-fucosidase, a- and b-galactosidase, a- and b-mannosidase, proteases: none detected.. EC 3.2.1.18, RTECS QQ3450000, CAS 9001-67-6. Note: 1 mU = 1 milliunit.

Ref.: Means, R.E. and Desrosiers, R.C. 2000. J. Virol. 74, 11181. Prime, S., et al. 1996. J. Chromatogr. A. 720, 263. Roggentin, P., et al. 1995. Biol. Chem. Hoppe Seyler 376, 569 Dwek, R.A., et al. 1993. Annu. Rev. Biochem. 62, 65.
R: 20-36/37/38-42/43; S: 26-36