NEU2
NEU2 (neuraminidase 2, also known as sialidase-2 or SIAL2) is a cytosolic exo-alpha-sialidase that removes terminal sialic acid from glycolipids, glycoproteins and oligosaccharides. It belongs to the glycosyl hydrolase 33 family and the neuraminidase gene group. Browse Assay Genie's current range of NEU2 research reagents below, or read on for the biology behind the target.
NEU2 catalyses the hydrolytic cleavage of the terminal sialic acid, N-acetylneuraminic acid (Neu5Ac), from the glycan moiety of glycolipids, glycoproteins and oligosaccharides, contributing to their catabolism. The enzyme recognises both the sialyl linkage position and the supramolecular organisation of the sialoglycoconjugate. It prefers alpha-(2->3)-sialylated GD1a and GT1B gangliosides over alpha-(2->8)-sialylated GD1b, in monomeric forms and in micelles. It hydrolyses monomeric GM1 ganglioside but has no activity towards the micellar form.
Activity towards glycoproteins such as fetuin and transferrin, which carry a mixture of alpha-(2->3) and alpha-(2->6) sialyl linkages, is lower. NEU2 cleaves the milk oligosaccharide alpha-(2->3)-sialyllactose but is inactive towards the alpha-(2->6)-sialyllactose isomer, and it does not act on colominic acid, a homomer of alpha-(2->8)-linked Neu5Ac residues. This linkage selectivity makes it a useful reference enzyme for studies of sialic acid biology.
The NEU2 gene belongs to a family of glycohydrolytic enzymes that remove sialic acid residues from glycoproteins and glycolipids. Expression studies in COS7 cells confirmed that it encodes a functional sialidase, and cell fractionation experiments demonstrated its cytosolic localisation. Previous names include sialidase 2 (cytosolic sialidase), and the mouse and rat orthologues are both designated Neu2. NEU1 is another member of the neuraminidase group.
NEU2 removes terminal Neu5Ac from glycolipids, glycoproteins and oligosaccharides, making it a focus for studies of sialoglycoconjugate breakdown.
The enzyme prefers alpha-(2->3)-sialylated GD1a and GT1B gangliosides and acts on monomeric GM1, which suits work on ganglioside substrate specificity.
NEU2 cleaves alpha-(2->3)-sialyllactose but not the alpha-(2->6) isomer, providing a model for how sialidases discriminate linkage type.
Cell fractionation showed that NEU2 is cytosolic, supporting research into sialidase compartmentalisation and the neuraminidase family.
NEU2 is an exo-alpha-sialidase that hydrolytically cleaves terminal sialic acid (Neu5Ac) from glycolipids, glycoproteins and oligosaccharides during their catabolism. It favours alpha-(2->3)-sialylated gangliosides such as GD1a and GT1B, and it is a cytosolic enzyme.
NEU2 stands for neuraminidase 2. UniProt names the protein sialidase-2, SIAL2 is an alias, and earlier HGNC names were sialidase 2 (cytosolic sialidase) and neuraminidase 2 (cytosolic sialidase). Its enzyme classification is EC 3.2.1.18, and it belongs to the glycosyl hydrolase 33 family.
Orthologues of the human NEU2 gene are designated Neu2 in both mouse and rat. Cross-species use of any reagent depends on the product, so check the datasheet of any product for its validated reactivity.
Other neuraminidase family members with research reagents at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q9Y3R4; product specifications from Assay Genie datasheets.