Not available outside of the UK & Ireland.

Application

Neuraminidase (Sialidase) has been used to desialylate transferrin in order to study its isoforms in human serum.

Use Neuraminidase to hydrolyze terminal N- or 0-acylneuraminic acids which are α2,3-, α2,6-, or α2,8-linked (rate α2,3: > α2,6 = α2,8) to oligosaccharides, polysaccharides, mucopolysaccharides, glycoproteins, and glycolipids.In contrast to the enzyme from Arthrobacter ureafaciens, neuraminidase from Clostridium perfringens hydrolyzes α2,3-linkages faster than α2,6-linkages. α2,8-bound sialic acids area cleaved with a similar velocity compared to α2,6-bound sialic acids.Neuraminidase is used for:Virus receptor studiesStudies on the interaction of lymphocytes with tumor cellsCell hybridizations Analysis of oligosaccharidesAnalysis of glycoproteinsAnalysis of glycolipids

Biochem/physiol Actions

Neuraminidase mediates apoptosis in the host cell before viral entry.

Neuraminidase breaks α-ketosidic linkage between N-acetylneuraminic acid and the adjacent sugar residue.

General description

Acylneuraminyl-hydrolase

Other Notes

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

Preparation Note

Stabilizers: The enzyme can be stabilized by bovine serum albumin (BSA).Storage conditions (working solution): After reconstitution in double-dist. water or sample buffer, the enzyme is stable for several weeks, stored at 2 to 8 °C; for longer storage, freezing is recommended. A stock solution may be made (e.g., at c = 5 U/100 µl). The enzyme looses approx. 50% of its activity after incubation at 37 °C for 24 hours.

Specificity

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 α2,3 >α2,8 = α2,6, determined on bonds in tri- and tetrasaccharides.