NEU2 Protein, Human (HEK293, His)

NEU2 protein acts as an exo-α sialidase and selectively hydrolyzes terminal sialic acids in glycolipids, glycoproteins, and oligosaccharides. It shows specificity for α-(2->3)-sialylated GD1a and GT1B gangliosides, preferring α-(2->3) over α-(2->8)-sialylated GD1b. NEU2 Protein, Human (HEK293, His) is the recombinant human-derived NEU2 protein, expressed by HEK293 , with C-His labeled tag. The total length of NEU2 Protein, Human (HEK293, His) is 380 a.a., with molecular weight of ~43.7 kDa.

The NEU2 Protein functions as an exo-alpha-sialidase, catalyzing the hydrolytic cleavage of terminal sialic acid in the catabolism of glycolipids, glycoproteins, and oligosaccharides. It demonstrates specificity for alpha-(2->3)-sialylated GD1a and GT1B gangliosides, showing preference over alpha-(2->8)-sialylated GD1b. While it hydrolyzes monomeric GM1 ganglioside, it lacks activity toward the miscellar form. NEU2 exhibits lower sialidase activity for glycoproteins like fetuin and TF/transferrin carrying a mixture of alpha-(2->3) and alpha-(2->6)-sialyl linkages. It cleaves milk oligosaccharide alpha-(2->3)-sialyllactose but remains inactive toward the alpha-(2->6)-sialyllactose isomer and colominic acid, a homomer of alpha-(2->8)-linked Neu5Ac residues.

Human

HEK293

C-His

Q9Y3R4 (M1-Q380)

4759  [NCBI]

Approximately 43.7 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.