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Galectin-14 (LGALS14) is a carbohydrate-binding protein classified within the prototype galectin family, characterized by a single carbohydrate recognition domain (CRD) per monomer and typically forming dimers[1][2][5]. It is predominantly expressed in the human placenta, where its levels surpass other galectins, indicating a specialized role in fetal development and regulation of maternal immune tolerance during pregnancy[1][2][3]. Galectin-14 can induce T-cell apoptosis and participate in protein-protein interactions, including colocalization with c-Rel, a member of the NF-κB family, suggesting potential influence on signal transduction pathways[1][2][3]. Structurally, it is distinct from other galectins, with low affinity for lactose due to noncanonical amino acid substitutions in its binding site[1][2]. Its main biological functions and disease associations center on reproductive and immunological processes, but there are no known approved drugs or specific drug interactions targeting this protein[3].
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