Galectin-8 (Gal-8) is a lectin family member and is one of the tandem repeat-type galectins containing two carbohydrate recognition domains (CRD) connected by a linker region in a single peptide chain. The CRD is responsible for β-galactoside binding, and the binding partners for galectin-8 have been identified, including CD44 and a subset of integrins. Galectin-8 and integrins form complexes, subsequently leading to phosphorylation of paxillin and focal adhesion kinase (FAK), which activates signal pathways including MAPK-ERK and PI3K-AKT pathways. Galectin-8 is constitutively presented in the Liver, kidney, cardiac muscle, lung, and brain. Galectin-8 serves as an immunosuppressive protective role against autoimmune CNS inflammation, regulating the balance of Th17 and Th1 polarization.