Anti-MAG

0.5mg/ml if reconstituted with 0.2ml sterile DI water. Myelin-associated glycoprotein, also known as SIGLEC4A, is a cell membrane glycoprotein that is a member of the SIGLEC family of proteins and is a functional ligand of the NOGO-66 receptor, NgR. It is though to be involved in the process of myelination. Cleavage of GPI-linked proteins from axons protects growth cones from MAG-induced collapse, and dominant-negative NgR eliminates MAG inhibition of neurite outgrowth. Resistant embryonic neurons were rendered sensitive by expression of NgR. The glycoprotein binds specifically to an NgR-expressing cell line in a GPI-dependent and sialic acid-independent manner. Experiments blocking NgR from interacting with the glycoprotein prevented inhibition of neurite outgrowth by MAG. In cultured human embryonic kidney (HEK) cells expressing the NOGO receptor, p75(NTR) was required for MAG-induced intracellular calcium elevation. Protein function: Adhesion molecule that mediates interactions between myelinating cells and neurons by binding to neuronal sialic acid- containing gangliosides and to the glycoproteins RTN4R and RTN4RL2. Not required for initial myelination, but seems to play a role in the maintenance of normal axon myelination. Protects motoneurons against apoptosis, also after injury, protection against apoptosis is probably mediated via interaction with neuronal RTN4R and RTN4RL2. Required to prevent degeneration of myelinated axons in adults, this probably depends on binding to gangliosides on the axon cell membrane. Negative regulator of neurite outgrowth, in dorsal root ganglion neurons the inhibition is mediated primarily via binding to neuronal RTN4R or RTN4RL2 and to a lesser degree via binding to neuronal gangliosides. In cerebellar granule cells the inhibition is mediated primarily via binding to neuronal gangliosides. In sensory neurons, inhibition of neurite extension depends only partially on RTN4R, RTN4RL2 and gangliosides. Inhibits axon longitudinal growth. Inhibits axon outgrowth by binding to RTN4R. Preferentially binds to alpha-2,3-linked sialic acid. Binds ganglioside Gt1b. [The UniProt Consortium]