Mouse 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:10713120).
Recognizes sialyl linkage positions of the glycan moiety as well as the supramolecular organization of the sialoglycoconjugate (By similarity).
Displays preference for alpha-(2->3)-sialylated GD1a and GT1B gangliosides over alpha-(2->8)-sialylated GD1b, in both monomeric forms and micelles (PubMed:10713120).
Hydrolyzes exclusively monomeric GM1 ganglioside, but has no activity toward the miscellar form (By similarity).
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 (By similarity).
Cleaves milk oligosaccharide alpha-(2->3)-sialyllactose, but is inactive toward isomer alpha-(2->6)-sialyllactose isomer.
Has no activity toward colominic acid, a homomer of alpha-(2->8)-linked Neu5Ac residues (By similarity).
{ECO:0000250|UniProtKB:Q9Y3R4, ECO:0000269|PubMed:10713120}.
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