Galectin-2 is a member of the galectin family, which consists of carbohydrate-binding proteins with a high affinity for β-galactosides. These proteins play crucial roles in various biological processes, including cell-cell adhesion, cell-matrix interactions, and immune responses. Galectin-2, in particular, has garnered interest due to its unique properties and potential therapeutic applications.
Galectin-2 is a homodimeric protein with a molecular weight of approximately 14 kDa . It shares structural similarities with galectin-1 but has a distinct expression profile. Unlike galectin-1, which is widely expressed in various tissues, galectin-2 is primarily confined to the gastrointestinal tract . This restricted expression pattern suggests specialized functions in this region.
The gene encoding galectin-2 is located on chromosome 22 in humans. The protein consists of a single carbohydrate recognition domain (CRD), which is responsible for its binding to β-galactosides . The amino acid sequence of human galectin-2 shares significant identity with its mouse and rat counterparts, indicating a conserved function across species .
Galectin-2 has been shown to play a role in various biological processes:
Recombinant human galectin-2 is typically produced using human embryonic kidney (HEK) 293 cells. The recombinant protein is purified to high levels of purity, often exceeding 95%, and is free from endotoxins . This high-quality recombinant protein is used in various research applications, including studies on cell adhesion, apoptosis, and immune regulation.
The unique properties of galectin-2, particularly its ability to induce apoptosis in activated T cells, make it a promising candidate for therapeutic applications. It could be explored as a treatment for autoimmune diseases, where the selective elimination of activated T cells is desirable. Additionally, its role in modulating immune responses opens avenues for its use in cancer immunotherapy and inflammatory diseases .