N2133 Sigma

Neuraminidase from Clostridium perfringens (C. welchii)

Type X, lyophilized powder, ≥50 units/mg protein (using NAN-lactose)

DOWNLOAD MSDS (PDF)

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

Description

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. 3

Preparation Note

Purified by affinity chromatography from Type VIII (N 5631)

Unit Definition

One unit will liberate 1.0 μmole of N-acetylneuraminic acid per min at pH 5.0 at 37 °C using NAN-lactose or bovine submaxillary mucin unless otherwise specified.

Application

Neuraminidase from Clostridium perfringens has been used in a study to assess purification via affinity chromatography. 1 It has also been used in a study to investigate site-directed mutations of amino acids of the neuraminidase gene, nanH. 2

Biochem/physiol Actions

Hydrolyzes α(2→3), α(2→6), and α(2→8)-glycosidic linkages of terminal sialic residues of various glycomolecules.

Neuraminidase can block attachment of type 3 reovirus to cell membranes. This effect is related to the ability of neuraminidase to hydrolysis sialic acid residues within cell surface receptors.

Price and Availability

Customers Also Viewed

recombinant, expressed in E. coli, buffered aqueous solution, ≥250 units/mg protein

α(2→3,6,8,9) Neuraminidase from <I>Arthrobacter ureafaciens</I>

Proteomics Grade, suitable for MALDI-TOF MS

Type VI, lyophilized powder, 6-10 units/mg protein (using NAN-lactose), 2-5 units/mg protein (mucin)

Type VIII, lyophilized powder, 10-20 units/mg protein (using NAN-lactose), 3.5-8.0 units/mg protein (mucin)

Technical Service:

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Bulk Ordering & Pricing:

Need larger quantities for your development, manufacturing or research applications?