oxidized recombinant human galectin-1

Oxidized recombinant human galectin-1 is a modified form of the protein galectin-1 produced via recombinant DNA technology. Galectin-1 is a member of the beta-galactoside-binding lectin family and plays key roles in cell-cell and cell-matrix interactions, immune regulation, apoptosis, and tissue repair. In its oxidized state—characterized by the formation of disulfide bonds between cysteine residues—galectin-1 loses its carbohydrate-binding (lectin) activity but gains new biological functions. Notably, oxidized recombinant human galectin-1 has been shown to promote axonal regeneration and enhance functional recovery after peripheral nerve injury in animal models. It increases both the number and diameter of regenerating myelinated fibers at sites distal to nerve transection[1][4][9]. The protein’s redox-dependent switch alters its structure and function; while reduced forms bind carbohydrates on cell surfaces to modulate immune responses or tumor progression[2], oxidation leads to loss of lectin activity but acquisition of neuroregenerative properties[5]. Recombinant production typically uses E. coli expression systems for research purposes.

Other names

oxidized galectin-1rhGAL-1/OxLGALS1 (oxidized form)