Recombinant Mouse Myelin-associated Glycoprotein/Siglec-4a (C-6His)
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| Amount : | 50 µg |
| Content : | Lyophilized from a 0.2 µm filtered solution of PBS,pH7.4. |
| AA sequence : | Recombinant Mouse Myelin-associated Glycoprotein is produced by our Mammalian expression system and the target gene encoding Gly20-Pro516 is expressed with a 6His tag at the C-terminus. |
| Alternative Name : | Myelin-Associated Glycoprotein; MAG; Siglec-4a |
Source : Human Cells;
Myelin-Associated Glycoprotein (MAG, Siglec-4a), is a type I transmembrane glycoprotein belonging to the Siglec family. It is composed of an extracellular segment containing five Ig-like domains, a single transmembrane segment, and a cytoplasmic domain. Mouse MAG shares 95% and 99% aa sequence identity with human and rat MAG, respectively. MAG functions as an adhesion molecule during neural development. It preferentially binds to alpha -2,3-linked sialic acid terminal structures found on cell surface molecules. MAG is selectively expressed by myelinating oligodendrocytes and Schwann cells and plays an important role in axon-myelin stability. MAG is also reported to regulate the axon cytoskeleton and support the distribution of axon molecules at the nodes of Ranvier. In addition, it has been identified as a major inhibitor of neurite outgrowth.
Myelin-Associated Glycoprotein (MAG, Siglec-4a), is a type I transmembrane glycoprotein belonging to the Siglec family. It is composed of an extracellular segment containing five Ig-like domains, a single transmembrane segment, and a cytoplasmic domain. Mouse MAG shares 95% and 99% aa sequence identity with human and rat MAG, respectively. MAG functions as an adhesion molecule during neural development. It preferentially binds to alpha -2,3-linked sialic acid terminal structures found on cell surface molecules. MAG is selectively expressed by myelinating oligodendrocytes and Schwann cells and plays an important role in axon-myelin stability. MAG is also reported to regulate the axon cytoskeleton and support the distribution of axon molecules at the nodes of Ranvier. In addition, it has been identified as a major inhibitor of neurite outgrowth.
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