Human sialidase 2 (NEU2) is a cytoplasmic sialidase that degrades sialyl glycoconjugates, including glycoproteins and gangliosides, via hydrolysis of terminal sialic acids to produce asialo-type molecules. It belongs to a family of glycohydrolytic enzymes that remove sialic acid residues from glycoproteins and glycolipids. NEU2 expression as assessed by quantitative real-time PCR was found to be extremely low or undetectable in many human tissues and cells, with notable exceptions like the placenta and testis. The human cytosolic sialidase NEU2 is the only mammalian enzyme structurally characterized and represents a valuable model to study the specificity of novel NA inhibitory drugs. Diseases associated with NEU2 include Galactosialidosis and Discrete Subaortic Stenosis.