NEU1
NEU1 (neuraminidase 1, also called sialidase-1 or NEU) is a lysosomal exo-alpha-sialidase that removes sialic acid residues from glycoproteins and glycolipids. It belongs to the glycosyl hydrolase 33 family and works as part of a multienzyme complex in the lysosome. Browse Assay Genie's current range of NEU1 research reagents below, or read on for the biology behind the target.
NEU1 is a lysosomal exo-alpha-sialidase that catalyses the removal of sialic acid (N-acetylneuraminic acid) moieties from glycoproteins and glycolipids. It appears to prefer alpha 2-3 and alpha 2-6 sialyl linkages. To be active, the enzyme is strictly dependent on its presence in a multienzyme complex. In the lysosome, NEU1 forms a heterotrimeric complex with beta-galactosidase and cathepsin A, the latter also referred to as protective protein.
The NEU1 gene encodes a protein of the glycosyl hydrolase 33 family, and HGNC places it in the neuraminidase gene group. UniProt records the NEU1 protein in the lysosome lumen and lysosome membrane, and also at the cell membrane. The mouse and rat orthologs are both named Neu1, which allows comparative work in rodent models. A related neuraminidase, NEU2, is a separate gene product.
Earlier HGNC names for the gene were sialidase 1 (lysosomal sialidase) and neuraminidase 1 (lysosomal sialidase), and NEU is a previous symbol. Mutations in the NEU1 gene can lead to sialidosis, a lysosomal storage disease. Type 1 (the cherry red spot-myoclonus syndrome, or normosomatic type) is late-onset. Type 2, the dysmorphic type, occurs at an earlier age with increased severity. This link makes NEU1 a central subject in studies of lysosomal sialic acid turnover.
Mutations in NEU1 cause sialidosis, so the enzyme is a focus for studying type 1 and type 2 lysosomal storage disease.
NEU1 cleaves terminal sialic acid from glycoproteins and glycolipids, making it relevant to studies of sialyl linkage processing.
NEU1 acts in a heterotrimeric complex with beta-galactosidase and cathepsin A, and its activity depends on that complex.
As a glycosyl hydrolase 33 family neuraminidase, NEU1 provides a reference point for comparing sialidase isoenzymes and their localisation.
NEU1 is a lysosomal exo-alpha-sialidase. It removes sialic acid (N-acetylneuraminic acid) from glycoproteins and glycolipids, with an apparent preference for alpha 2-3 and alpha 2-6 linkages. It is active only within a multienzyme complex that also contains beta-galactosidase and cathepsin A.
NEU1 is also known as sialidase-1 and neuraminidase 1. HGNC lists earlier names as sialidase 1 (lysosomal sialidase) and neuraminidase 1 (lysosomal sialidase), and NEU as a previous symbol. The enzyme is classified as EC 3.2.1.18 and sits in the neuraminidase gene group.
Mutations in the NEU1 gene can lead to sialidosis, a lysosomal storage disease with a late-onset type 1 and a more severe, earlier type 2. Mouse and rat both carry a Neu1 ortholog; check the datasheet of any product for its validated reactivity.
Other neuraminidase family members and neuronal targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q99519; product specifications from Assay Genie datasheets.