Human Sialidase-2, NEU2 ELI
3,140.00 ₪
Exo-alpha-sialidase that catalyzes the hydrolytic cleavage of the terminal sialic acid (N-acetylneuraminic acid, Neu5Ac) of a glycan moiety in the catabolism of glycolipids, glycoproteins and oligosacharides (PubMed: 14613940, PubMed: 22228546).
Recognizes sialyl linkage positions of the glycan moiety as well as the supramolecular organization of the sialoglycoconjugate.
Displays preference for alpha-(2->3)-sialylated GD1a and GT1B gangliosides over alpha-(2->8)-sialylated GD1b, in both monomeric forms and micelles.
Hydrolyzes monomeric GM1 ganglioside, but has no activity toward the miscellar form (PubMed: 14613940).
Has lower sialidase activity for glycoproteins such as fetuin and TF/transferrin that carry a mixture of alpha-(2->3) and alpha-(2->6)-sialyl linkages.
Cleaves milk oligosaccharide alpha-(2->3)-sialyllactose, but is inactive toward alpha-(2->6)-sialyllactose isomer.
Has no activity toward colominic acid, a homopolymer of alpha-(2->8)-linked Neu5Ac residues (PubMed: 14613940).
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