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N3001 Sigma

Neuraminidase from Clostridium perfringens (C. welchii)

Type VI, lyophilized powder, 6-10 units/mg protein (using 4MU-NANA), 2-5 units/mg protein (mucin)

Synonym: Acyl-neuraminyl Hydrolase, Receptor-destroying enzyme, Sialidase

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Properties

Related Categories 3.2.x.x Glycosidases, 3.x.x.x Hydrolases, Application Index, Biochemicals and Reagents, Carbohydrate Hydrolysis,
type   Type VI
form   lyophilized powder
composition   Protein, ≥50% biuret
foreign activity   Protease and NAN-aldolase, present
storage temp.   −20°C
Gene Information   Clostridium perfringens str. 13 ... nanI(988807)

Description

Analysis Note

Package sizes based on 4MU-NANA units

Package sizes based on the 4MU-NANA units

General description

Neuraminidase enzymes are hydrolase enzymes that promote influenza virus release from infected cells and facilitate virus spread.

Packaging

4, 10 units in glass bottle

Preparation Note

Chromatographically purified from Type V (N 2876)

Application

Neuraminidase from Clostridium perfringens (C. welchii) has been used in a study to assess a glycoprotein faction suitable for use as a substrate in preparation assays. It has also been used in a study to investigate the action of an epsilion-toxin on MDCK cells.

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.

Neuraminidase from Clostridium perfringens reduces the viability of human leukemic myeloblasts and attenuates their ability to activate lymphocytes.

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.

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.

Price and Availability

Suggested Laboratory Gloves


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Available in ELITE Grade
Safety & Documentation

Safety Information

RIDADR 
NONH for all modes of transport
WGK Germany 
3
RTECS 
QQ3450000
Protocols & Articles

Protocols

Enzymatic Assay of Neuraminidase

2.1. This procedure applies to products that have a specification for neuraminidase content by enzymatic determination.

Related Content

Enzymes & Proteins

Application Index | Enzyme Index | Substrate Index | Inhibitor Index | Cofactor Index | Lectin Index
Keywords: Cell signaling, Diagnostic, Drug discovery, Molecular biology

Peer-Reviewed Papers
15

References

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M8639 2′-(4-Methylumbelliferyl)-α-D-N-acetylneuraminic acid sodium salt hydrate, ≥95% (HPLC)
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