The protein encoded by this gene is a type I membrane protein and member of the immunoglobulin superfamily. It is thought to be involved in the process of myelination. It is a lectin that binds to sialylated glycoconjugates and mediates certain myelin-neuron cell-cell interactions. Two alternatively spliced transcripts encoding different isoforms have been described for this gene. (provided by RefSeq)
Immunogen
MAG (NP_002352, 119 a.a. ~ 208 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Monoclonal Anti-MAG antibody produced in mouse is suitable for immunohistochemistry (formalin-fixed, paraffin-embedded sections), indirect ELISA, and western blot applications.
Biochem/physiol Actions
Myelin-associated glycoprotein (MAG) is a glycoprotein with five Ig-like domains belonging to the siglec family of molecules (sialic acid-binding, immunoglobulin-like lectins). It is highly involved in the myelin formation and its maintenance. It is expressed in oligodendrocyte processes at the axoglial junction. It possesses sialic acid binding affinity. Deletion of MAG region leads to Kearns-Sayre syndrome characterized with oligodendrocyte loss and nuclear translocation of apoptosis-inducing factor. MAG also has been reported as an important inhibitor of axonal regeneration.
Physical form
Solution in phosphate buffered saline, pH 7.4
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Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 27(34), 9146-9154 (2007-08-24)
Myelin-associated glycoprotein (MAG) is a potent inhibitor of axonal regeneration. It contains five Ig-like domains and is a sialic binding protein. Previously, we showed that the sialic acid binding site on MAG maps to arginine 118 in Ig domain 1
Archives of neurology, 69(4), 490-499 (2012-04-12)
To explore myelin components and mitochondrial changes within the central nervous system in patients with well-characterized mitochondrial disorders due to nuclear DNA or mitochondrial DNA (mtDNA) mutations. Immunohistochemical analysis, histochemical analysis, mtDNA sequencing, and real-time and long-range polymerase chain reaction
NG2-glia are highly proliferative oligodendrocyte precursor cells (OPCs) that are widely distributed throughout the central nervous system (CNS). During development, NG2-glia predominantly differentiate into oligodendrocytes (OLs) to myelinate axon fibers, but they can also remain as OPCs persisting into the
COUP-TFII plays a role in cAMP-induced Schwann cell differentiation and in vitro myelination by up-regulating Krox20.
Han, et al.
Journal of Neurochemistry, 165, 660-681 (2023)
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