MAG/Siglec-4a Protein, Human (Biotinylated, HEK293, His-Avi)

The MAG/Siglec-4a protein serves as an adhesion molecule facilitating interactions between myelinating cells and neurons by binding to neuronal sialic acid-containing gangliosides, as well as the glycoproteins RTN4R and RTN4RL2. Although not essential for initial myelination, MAG/Siglec-4a appears to play a crucial role in maintaining normal axon myelination and protecting motoneurons against apoptosis, particularly after injury. This protective effect is likely mediated through interactions with neuronal RTN4R and RTN4RL2. In adults, MAG/Siglec-4a is required to prevent degeneration of myelinated axons, possibly relying on binding to gangliosides on the axon cell membrane. Acting as a negative regulator of neurite outgrowth, MAG/Siglec-4a inhibits axon longitudinal growth and outgrowth by preferentially binding to alpha-2,3-linked sialic acid and interacting with RTN4R, RTN4RL2, and gangliosides. The protein exists as both a monomer and homodimer, and its interactions extend to include isoform 2 of BSG, contributing to its intricate role in modulating neuronal responses and axonal dynamics.