Glycoprotein-9 (GP9), also known as Galectin-9 (Gal-9), is a member of the galectin family of proteins. These proteins are characterized by their ability to bind to specific carbohydrate structures on glycoproteins and glycolipids. Galectin-9 is known for its diverse roles in various physiological and pathological processes, including immune response modulation, cell adhesion, and apoptosis.
Galectin-9 is a tandem-repeat type galectin, meaning it has two carbohydrate recognition domains (CRDs) connected by a linker peptide. This structure allows Galectin-9 to cross-link glycoproteins on the cell surface, leading to various cellular responses. The protein is involved in several key functions:
Human recombinant Galectin-9 is produced using recombinant DNA technology. This involves inserting the gene encoding Galectin-9 into a suitable expression system, such as bacteria or mammalian cells, to produce the protein in large quantities. The recombinant protein is then purified for use in research and therapeutic applications.
Galectin-9 has been extensively studied for its potential therapeutic applications: