Description
General description
Calorimetry studies show that the two lectin-like domains flanking the central catalytic domain of Neuraminidase serve as the recognition and binding sites for sialic acid-containing substrates.
Neuraminidase enzymes are hydrolase enzymes that promote influenza virus release from infected cells and facilitate virus spread.
Application
Neurminidase is used as a cell-surface probe for glycoconjugate distribution and in substrate specificity studies.
Neuraminidase from Vibrio cholera has been used in a study to describe a five-step purification method. It has also been used in a study to investigate modification of leukemia L1210 tumor cells.
Physical form
Solution in 50 mM sodium acetate, pH 5.5, containing 0.15 M sodium chloride and 4 mM calcium chloride, 0.2 μm filtered..
Preparation Note
A further purification by affinity chromatography of our Type III.
Analysis Note
Preservative free.
Other Notes
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. Prices based on units using NAN-lactose as substrate.