Galectins comprise a family of multifunctional carbohydrate-binding proteins with specificity for N‑acetyl-lactosamine-containing glycoproteins. At least 14 mammalian Galectins share structural similarities in their carbohydrate recognition domains (CRD), forming three groups: prototype (one CRD), tandem-repeat (two CRDs), and chimeric (one CRD, unique N‑terminus) (1, 2). Full length Galectin-9 is a widely expressed 39 kDa tandem-repeat Galectin that contains two CRDs connected by a linker region (3). Progressive deletion within the linker region generates a 36 kDa isoform, also known as Ecalectin or UAT, as well as a 35 kDa isoform (4). This recombinant protein corresponds to the Ecalectin isoform of human Galectin-9 and shares 70% and 73% aa sequence identity with the corresponding regions of mouse and rat Galectin-9, respectively. Galectin-9 exhibits a wide range of activities. All three isoforms function as eosinophil chemoattractants (5, 6). This activity is destroyed by thrombin-mediated cleavage within the linker region of the long isoform, although the Ecalectin isoform is resistant to thrombin (7). Galectin-9 binds to carbohydrate moieties of IgE, thereby preventing immune complex formation, mast cell degranulation, and asthmatic and cutaneous anaphylaxis reactions (8). Independent of its lectin properties, Galectin-9 induces the maturation of dendritic cells which promote Th1 polarization (9). Galectin-9 induces cellular apoptosis in part by direct binding to TIM-3 (10, 11). Its interaction with TIM-3 inhibits Th1 cell and CD8⁺ cytotoxic T cell responses and also promotes regulatory T cell differentiation and activity (11, 12). Galectin-9 suppresses tumor cell metastasis by interfering with the associations between hyaluronic acid and CD44 and between VCAM-1 and Integrin alpha 4 beta 1 (13). The Ecalectin isoform (UAT; urate transporter) can also be expressed as an integral membrane protein and mediate the cellular efflux of urate (14).