Neuraminidase-1 Recombinant Rabbit mAb (S-4004-109)

Neuraminidase-1 (NEU1), also known as lysosomal sialidase or sialidase-1, is the most abundantly expressed member of the mammalian sialidase family, encoded by the NEU1 gene located on chromosome 6p21.33. Structurally, NEU1 adopts a six-bladed β-propeller fold characteristic of the GH33 glycoside hydrolase family, with its active site situated in a central cavity. Within the lysosome, NEU1 functions as part of a heterotrimeric complex together with β-galactosidase and the protective protein/cathepsin A (PPCA), the latter serving as a molecular chaperone essential for NEU1's catalytic activation, lysosomal targeting, and stability. As an exo-sialidase, NEU1 cleaves terminal sialic acid residues from glycoproteins and glycolipids, thereby participating in the catabolism of sialoglycoconjugates. Beyond its classical lysosomal catabolic role, NEU1 can also be targeted to the cell surface, where it functions as a structural and functional modulator of multiple cellular receptors through desialylation, either activating or inhibiting them. At the plasma membrane, NEU1 associates with the elastin-binding protein and PPCA to form the elastin receptor complex, and its activation is required for elastogenesis and signal transduction mediated by elastin-derived peptides. NEU1 deficiency caused by NEU1 gene mutations leads to sialidosis, a lysosomal storage disorder characterized by the accumulation of sialylated oligosaccharides and glycoproteins, with type I presenting as the late-onset cherry-red spot-myoclonus syndrome and type II manifesting earlier with more severe dysmorphic features. Increasing evidence implicates NEU1 in the pathogenesis of various diseases, including multiple cancers (hepatocellular carcinoma, pancreatic carcinoma, and breast cancer), metabolic disorders such as obesity and insulin resistance, cardiovascular diseases, and inflammatory processes after myocardial ischemia/reperfusion, making it a pharmacological target of high potential.