NEU1 Human

Sialidase 1, also known as NEU1, is a lysosomal enzyme that plays a crucial role in the catabolism of sialic acids. Sialic acids are terminal acidic monosaccharides that influence the chemical and biological properties of glycoconjugates. The removal of sialic acids by sialidase modulates various biological processes by altering the conformation and binding sites of functional molecules .

Sialidase 1 belongs to the N-acetyl-α-neuraminidase family and is encoded by the NEU1 gene. It is expressed in many tissues, with high expression in the pancreas and weak expression in the brain . The enzyme is a part of a multienzyme complex that includes Cathepsin A (protective protein), β-galactosidase, and N-acetylgalactosamine-6-sulfate sulfatase .

Sialidase 1 catalyzes the removal of sialic acid residues from glycoproteins and glycolipids. This enzymatic activity is essential for the proper functioning of lysosomal catabolism. The enzyme has a preference for α2-3 and α2-6 sialyl linkages . The activity of Sialidase 1 is strictly dependent on its presence in the multienzyme complex .

Deficiencies in Sialidase 1 lead to sialidosis, a rare lysosomal storage disease characterized by the accumulation of sialylated glycoproteins and glycolipids in tissues . This condition manifests in various symptoms, including developmental delay, myoclonus, and vision problems.

Recombinant Human Sialidase 1 is produced using various expression systems, including yeast, E. coli, baculovirus, and mammalian cells . The recombinant protein is often tagged with His-tag for purification purposes and is supplied as a filtered solution for research use .