Recombinant Human NEU3 protein

NEU3. also known as sialidase 3. is a membrane-associated glycoprotein belonging to the neuraminidase family. It plays a critical role in modulating cellular processes by catalyzing the removal of terminal sialic acid residues from glycoproteins and glycolipids, thereby regulating cell signaling, adhesion, and proliferation. Dysregulation of NEU3 has been implicated in various pathologies, including cancer progression, neurodegenerative disorders, and metabolic diseases. For instance, its overexpression is linked to enhanced oncogenic signaling in colorectal, renal, and prostate cancers, while reduced activity is associated with neurodegenerative conditions like Alzheimer’s disease.

Recombinant NEU3 protein is engineered through genetic recombination techniques to enable large-scale production for research and therapeutic applications. Typically expressed in prokaryotic (e.g., *E. coli*) or eukaryotic systems (e.g., mammalian or insect cells), recombinant NEU3 retains enzymatic activity and structural integrity, allowing studies on its substrate specificity, inhibitor screening, and molecular interactions. Eukaryotic expression systems are often preferred to ensure proper post-translational modifications critical for functional studies.

The development of recombinant NEU3 has advanced drug discovery efforts, particularly in targeting sialidase-related pathways for cancer therapy or neuroprotection. It also serves as a tool to investigate sialic acid metabolism’s role in immune regulation and pathogen-host interactions. Structural studies using recombinant NEU3 have further elucidated its catalytic mechanism and binding sites, guiding the design of selective inhibitors. Despite progress, challenges remain in optimizing stability and activity for clinical applications, underscoring the need for continued research into its biology and therapeutic potential.