Galectin-3 Antibody (YA5606)

Galectin-3 is a β-galactoside-binding lectin that regulates cell adhesion, activation, migration, signaling, apoptosis, immune reactions, and neoplastic transformation^[1][2]. Mechanistically, its conserved carbohydrate-recognition domain binds β-galactosides, while its intrinsically disordered N-terminal region enables multisite self-association and functional multivalency^[1][2]. In inflammation, galectin-3 acts across acute inflammation, chronic inflammation, and tissue fibrogenesis, making it relevant to fibrosis-oriented experimental design^[3]. In lung fibrosis models, galectin-3 deficiency or pharmacological inhibition reduced TGF-β1-driven epithelial-mesenchymal transition, myofibroblast activation, and collagen production^[4]. More recent human lung fibroblast and IPF lung-slice data show that extracellular galectin-3 promotes integrin-mediated TGF-β1 activation and interacts with αv integrins and TGFβRII in a glycosylation-dependent manner^[5]. Compared with related isoforms, galectin-3 is distinguished as the only vertebrate chimera-type galectin, containing one CRD linked to a long proline- and glycine-rich N-terminal domain^[1]. For experimental applications, galectin-3 inhibitors that target the carbohydrate-recognition domain blocked integrin colocalization and reduced fibrotic mediators in IPF-derived lung tissue models^[5]. In patients with idiopathic pulmonary fibrosis, inhaled TD139 showed target engagement and supported galectin-3 inhibition as a translational research approach^[6].- Isoform distinction: galectin-3 differs structurally from prototype and tandem-repeat galectins through its chimera architecture^[1]. - Research application: galectin-3 inhibition supports fibrosis studies involving TGF-β1 activation, integrins, and IPF models^[4][5][6].