Neuraminidase (Sialidase)
ROCHE/11585886001 - from Clostridium perfringens
Synonym: Sialidase
Product Type: Chemical
| biological source | bacterial (Clostridium perfringens) |
| form | lyophilized |
| manufacturer/tradename | Roche |
| mol wt | 60 kDa |
| optimum pH | 5 |
| packaging | pkg of 5 U |
| Quality Level | 100  |
| shipped in | wet ice |
| specific activity | 100 U/mg |
| ~100 units/mg protein | |
| storage temp. | 2-8°C |
| Application: | Neuraminidase (Sialidase) has been used to desialylate transferrin in order to study its isoforms in human serum. |
| Application: | 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 studies • Studies on the interaction of lymphocytes with tumor cells • Cell hybridizations • Analysis of oligosaccharides • Analysis of glycoproteins • Analysis of glycolipids |
| Biochem/physiol Actions: | 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. |
| Biochem/physiol Actions: | Neuraminidase breaks α-ketosidic linkage between N-acetylneuraminic acid and the adjacent sugar residue. |
| Biochem/physiol Actions: | Neuraminidase mediates apoptosis in the host cell before viral entry. |
| General description: | approximately 100 U/mg protein at +37°C and pH 5.0 with N-acetyl-neuraminosyl-D-l |
| 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. |
| RIDADR | NONH for all modes of transport |
| WGK Germany | WGK 1 |
| Flash Point(F) | does not flash |
| Flash Point(C) | does not flash |
| activity | specific activity: 100 U/mg; specific activity: ~100 units/mg protein |
| Storage Temp. | 2-8°C |
| Enzyme Commission (EC) Number | 3.2.1.18 ( BRENDA  | IUBMB ) |
| UNSPSC | 12352204 |