Monoclonal antibody is produced by immunizing animals with recombinant human galectin-9 protein.
Galectins are a family of β-galactose binding proteins that are characterized by an affinity for poly-N-acetyllactosamine-enriched glycoconjugates and a carbohydrate-binding site (1,2). Members of the galectin family have been implicated in a variety of biological functions, including cell adhesion (3), growth regulation (4), cytokine production (5), T-cell apoptosis (6), and immune responses (7).
Galectin-9 is induced by proinflammatory stimuli, including IFN-γ, TNF-α, and TLR ligands, and regulates various immune responses through interaction with its ligand TIM-3 (8, 9). Binding of galectin-9 to TIM-3 expressed by Th1 CD4 T cells resulted in T cell death (9). On the other hand, galectin-9 treatment of tumor-bearing mice increased the number of IFN-γ-producing TIM-3+ CD8 T cells and TIM-3+ dendritic cells (10). Transgenic overexpression of either TIM-3 or galectin-9 in mice led to an increase in cells with a myeloid-derived suppressor cell phenotype and inhibition of immune responses (11). CD44 is also proposed to be a receptor for galectin-9, and interaction of galectin-9 with CD44 expressed by induced regulatory T (iTreg) cells enhanced the stability of function of iTreg cells. In addition, galectin-9 was recently demonstrated to bind Dectin-1 expressed by pancreatic ductal adenocarcinoma-infiltrating macrophages, resulting in tolerogenic macrophage reprogramming and suppression of anti-tumor immunity. Increased galectin-9 expression has been observed in several cancer types, including lung, liver, breast, and kidney (12). Alternative splicing of the galectin-9 transcript leads to several isoforms (13).
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