Neuraminidase from Clostridium perfringens (C. welchii)
SIGMA/N5631 - Type VIII, lyophilized powder, 10-20 units/mg protein (using 4MU-NANA), 3.5-8.0 units/mg protein (mucin)
Synonym: Acyl-neuraminyl Hydrolase; Receptor-destroying enzyme; Sialidase
CAS Number: 9001-67-6
EC Number: 232-624-6
MDL Number: MFCD00131711
Product Type: Chemical
Neuraminidase non-specific cleavage for sialic acid — α(2-3), α(2-6) and α(2-8) glycosiduic linkages with a variety of natural and synthetic substrates
This picture is provided solely for illustration purposes. Optical properties of the actual product may deviate. Relevant product information is printed on labeled products and other accompanying or available information material. This image depicts SKU: N5631-5UN
| composition | Protein, ≥85% biuret |
| foreign activity | Protease and NAN-aldolase, present |
| form | lyophilized powder |
| Quality Level | 200  |
| specific activity | 10-20 units/mg protein (using 4MU-NANA) |
| 3.5-8.0 units/mg protein (mucin) | |
| storage temp. | −20°C |
| type | Type VIII |
| Analysis Note: | Package sizes based on 4MU-NANA units |
| Analysis Note: | Package sizes based on the 4MU-NANA units |
| Application: | Neuraminidase from Clostridium perfringens has been used in a study to assess the binding characteristics of iota toxin by fluorescence-activated cytometry. It has also been used in a study to investigate the distribution of neuraminidase among food poisoning strains. |
| Biochem/physiol Actions: | Neuraminidase cleavage of sialic acid groups has been used to study recognition by antibodies of glycoprotein structures. The use of neuraminidase in the estimation of N-acetylneuraminic acid was compared favorably to two other methods. |
| Biochem/physiol Actions: | Neuraminidases are used to cleave terminal N-acetyl neuraminic acid (sialic acid) from a variety of glycoproteins. The enzyme from Clostridium perfringens cleaves terminal sialic acid residues which are α-2,3- α-2,6- or α-2,8-linked to Gal, GlcNac, GalNAc, AcNeu, GlcNeu, oligosaccharides, glycolipids or glycoproteins. The relative rate of cleavage decreases in the order: α-2-3 > α-2-6 . α-2-8. Neuraminidase from C. perfringens cleaves α-2-3 linked sialic acid residues most efficiently, compared to A. ureafaciens, (Sigma N3642) which preferentially cleaves α-2-6 linked residues. |
| Biochem/physiol Actions: | The degradation of gangliosides grown in lipid mono layers by Clostridium perfringens neuraminidase depends largely on surface pressure. Increased pressure can inhibit neuraminidase activity. |
| Biochem/physiol Actions: | The use of neuraminidase to remove sialic acid residues from glycoproteins on cell surfaces has been frequently reported. Generally, procedures have indicated using neuraminidase in PBS at 37°C for 30 minutes, followed by several washings with PBS. Treatment of tissue sections with neuraminidase at much lower concentrations require longer incubation: for 1-4 U/mL in 0.1 M acetate buffer pH 4.2-5, from 2 to 20 hours at 37 °C. |
| General description: | Neuraminidase enzymes are glycoside hydrolase enzymes that catalyze hydrolysis of terminal sialic acid residues. The most well-known are the viral nearamidases, which promote influenza virus release. |
| Other Notes: | One unit will liberate 1.0 micromole of N-acetyl neuraminic acid per minute at pH 5.0 at 37 °C using bovine submaxillary mucin. One unit will hydrolyze 1.0 micromole of 2′-(4-methylumbelliferyl) |
| Preparation Note: | Chromatographically purified from Type V (N 2876) |
| RIDADR | NONH for all modes of transport |
| WGK Germany | WGK 3 |
| Flash Point(F) | Not applicable |
| Flash Point(C) | Not applicable |
| activity | specific activity: 10-20 units/mg protein (using 4MU-NANA); specific activity: 3.5-8.0 units/mg protein (mucin) |
| Storage Temp. | −20°C |
| Enzyme Commission (EC) Number | 3.2.1.18 ( BRENDA  | IUBMB ) |
| UNSPSC | 12352204 |