Galectin-8/LGALS8 (F9O3T) Rabbit mAb #45586

Galectins are a family of β-galactose binding proteins with intracellular and extracellular activities regulating cell adhesion and migration, immune responses, inflammation, cell death, and proliferation and are linked to several pathological conditions (reviewed in 1). Galectins can be divided into three groups: 1) prototype galectins (Gal-1, -2, -5, -7, -10, -11, -13, and -16) having one carbohydrate-recognition domain (CRD); 2) tandem-repeat type galectins (Gal-4, -6, -8, -9, and -12) that have two CRDs joined by a linker peptide; and 3) a chimera-type (Gal-3) that has a single CRD joined to an N-terminal non-lectin domain.

Galectin-8 (Gal-8; gene name LGALS8), which belongs to the group of tandem-repeat galectins, is important in adaptive and innate immunity with significant roles in host defense as well as tumor progression (reviewed in 2,3). Extracellular galectin-8 promotes cell adhesion through interaction with several cell surface proteins, including integrins (4,5), CD44 (6), CD45 (7), and CD166 (8). Intracellular galectin-8 binds to farnesylated K-Ras4B, regulating MAPK signaling (9). It also exerts a role in xenophagy by binding to glycans exposed on bacterial pathogens and recruiting NDP52 for destruction by autophagy, thereby restricting bacterial proliferation (10,11). Abundant expression of galectin-8 has been observed in various cancer types and, in some cases, associated with poor prognosis (12-14).