Neuraminidase (Sialidase)

For the hydrolysis of glycolipids, the presence of a detergent is necessary. Because of the broad substrate specificity, the enzyme is very well suited for the complete removal of sialic acids from glycoconjugates of a wide variety of biological materials.

Neuraminidase has been used for the:

• detection of the cell surface glycosylations in human anaplastic large cell lymphoma cells
• release of sialic acid from cells
• antibody-overlay lectin microarray

Cleaves terminal sialic-acid residues that are α2,3-, α2,6-, or α2,8-linked to Gal, GlcNAc, GalNAc, AcNeu, GlcNeu, oligosaccharides, glycolipids, or glycoproteins. Relative rate of cleavage is α2,6 >α2,3 >α2,8, determined on bonds in tri- and tetrasaccharides.

Neuraminidase hydrolyzes terminal N- or O-acylneuraminic acids which are α2,3-, α2,6-, or α2,8-linked (rate: α2,6 > α2,3 > α2,8) to oligosaccharides, polysaccharides, mucopolysaccharides, glycoproteins, and glycolipids. Noteworthy, for the hydrolysis of glycolipids, the presence of a detergent is necessary. Because of the broad substrate specificity, the enzyme is very well suited for the complete removal of sialic acids from glycoconjugates of a wide variety of biological materials.

This product is a mixture of isoenzymes (L, M1, M2 and S) with the following molecular weight values: ~ 52 kDa, 66 kDa and 88 kDa.

For life science research only. Not for use in diagnostic procedures.

Solution in 10 mM sodium phosphate, 0.1% Micr-O-Protect (w/v), 0.25 mg/ml bovine serum albumin, pH 7

Working concentration: Enzyme/substrate ratio should be in the range of 0.04 U/25-80 μg.