M5063
Myelin-Associated Glycoprotein/Fc Chimera from rat
>95% (SDS-PAGE), recombinant, expressed in NSO cells, lyophilized powder
Synonyme(s) :
MAG
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About This Item
Produits recommandés
Source biologique
rat
Niveau de qualité
Produit recombinant
expressed in NSO cells
Essai
>95% (SDS-PAGE)
Forme
lyophilized powder
Poids mol.
120 kDa by SDS-PAGE
calculated mol wt ~81 kDa
Impuretés
endotoxin, tested
Numéro d'accès UniProt
Application(s)
cell analysis
Température de stockage
−20°C
Informations sur le gène
rat ... Mag(29409)
Catégories apparentées
Actions biochimiques/physiologiques
MAG is a type I transmembrane glycoprotein containing five Ig-like domains in its extracellular domain. It is an adhesion molecule belonging to the immunoglobin superfamily. These adhesion molecules bind specifically to cell-surface glycan containing sialic acid residues that define the I-type sialyl lectin subgroup. Thus, they are also called the sialoadhesin family. Sialoadhesins mediate diverse biological processes through recognition of specific sialyted glycans on the cell surface. MAG, a minor component of myelin in the central and peripheral nervous system, has been implicated in the formation and maintenance of myelin. MAG is expressed on myelinating oligodenrocytes and Schwann cells, and preferentially recognize a 2,3-linked sialic acid on O-linked glycans and gangliosides. MAG exists as two isoforms that differ in the sequence and length of the cytoplasmic tail. The large isoform (71 kDa) and small isoform (67 kDa) arise from alternative splicing of mRNAs. Lymphocytes under pathologic conditions, it would normally interact with neuronal cells. It has been shown that MAG promotes axonal growth from neonatal dorsal root ganglion (DRG) neurons and embryonic spinal neurons, but is a potent inhibitor of axonal re-growth from adult DRG and postnatal cerebellar neurons. MAG plays an important role in the interaction between axons and myelin. A soluble form of MAG containing the extracellular domain is released from myelin in large quantities and identified in normal human tissues and in tissues from patients with neurological disorders. This soluble MAG may contribute to the lack of neuronal regeneration after injury.
MAG, a member of the immunoglobin superfamily, is expressed on myelinating oligodendrocytes and Schwann cells. MAG plays an important role in the interacation between axons and myelin.
Autres remarques
Extracellular domain of rat myelin-associated glycoprotein (MAG) fused to the C-terminal Fc region of human IgG1.
Forme physique
Lyophilized from a 0.2 μm filtered solution in phosphate buffered saline.
Remarque sur l'analyse
Measured by its ability to inhibit neurite outgrowth of cultured embryonic chick dorsal root ganglia neurons.
Code de la classe de stockage
13 - Non Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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J L Salzer et al.
The Journal of cell biology, 104(4), 957-965 (1987-04-01)
The myelin associated glycoproteins (MAG) are integral plasma membrane proteins which are found in oligodendrocytes and Schwann cells and are believed to mediate the axonal-glial interactions of myelination. In this paper we demonstrate the existence in central nervous system myelin
S Kelm et al.
Current biology : CB, 4(11), 965-972 (1994-11-01)
Protein-carbohydrate interactions are believed to be important in many biological processes that involve cell-cell communication. Apart from the selectins, the only well-characterized vertebrate sialic acid-dependent adhesion molecules are CD22 and sialoadhesin; CD22 is a member of the immunoglobulin superfamily that
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