Galectin-1 is a member of the galectin family, which consists of carbohydrate-binding proteins with a high affinity for β-galactoside-containing glycoconjugates. This protein is encoded by the LGALS1 gene and is characterized by its ability to bind to specific sugar moieties on the surfaces of cells and within the extracellular matrix .
Galectin-1 is a 135 amino acid, 14 kDa protein that can exist as a monomer or homodimer. It lacks a classical signal peptide, which means it can be localized to the cytosolic compartments or secreted via non-classical pathways . The recombinant form of mouse Galectin-1 is typically produced in Escherichia coli and purified to a high degree of purity, often greater than 95% as determined by SDS-PAGE .
Galectin-1 plays a crucial role in various biological processes, including cell-cell adhesion, cell-matrix interactions, and immune response modulation. It has been shown to have immunosuppressive and anti-inflammatory properties, making it a key player in the resolution of acute and chronic inflammation . Galectin-1 can inhibit the synthesis of proinflammatory cytokines, reduce neutrophil trafficking, and suppress mast cell degranulation .
Due to its broad anti-inflammatory and immunomodulatory activities, Galectin-1 has been studied for its potential therapeutic applications in various diseases. These include autoimmune diseases, allergic inflammation, cancer, and infections . Therapeutic strategies targeting Galectin-1 interactions with glycans could help overcome cancer immunosuppression and enhance antimicrobial immunity .
Recombinant mouse Galectin-1 is widely used in research to study its biological functions and therapeutic potential. It is often used in cell culture experiments, ELISA assays, and other biochemical analyses. The protein is typically lyophilized and reconstituted in sterile PBS for use in various experimental setups .