Recombinant Human Galectin-3/LGALS3 Protein

The Galectin family of proteins consists of beta-galactoside binding lectins containing homologous carbohydrate recognition domains (CRDs). They also possess hemagglutination activity; which is attributable to their bivalent carbohydrate binding properties. Galectins are active both intracellularly and extracellularly. They have diverse effects on many cellular functions including adhesion; migration; polarity; chemotaxis; proliferation; apoptosis; and differentiation. Galectins may therefore play a key role in many pathological states; including autoimmune diseases; allergic reactions; inflammation; tumor cell metastasis; atherosclerosis; and diabetic complications. The galectins have been classified into the prototype galectins (1; 2; 5; 7; 10; 11; 13; 14); which contain one CRD and exist either as a monomer or a noncovalent homodimer. The chimera galectins (Galectin3) containing one CRD linked to a nonlectin domain; and the tandem repeat Galectins (4; 6; 8; 9; 12) consisting of two CRDs joined by a linker peptide. Galectins lack a classical signal peptide and can be localized to the cytosolic compartments where they have intracellular functions. However; via one or more as yet unidentified nonclassical secretory pathways; galectins can also be secreted to function extracellularly. Individual members of the galectin family have different tissue distribution profiles and exhibit subtle differences in their carbohydrate-binding specificities. Each family member may preferentially bind to a unique subset of cell surface glycoproteins.