Recombinant Rat MAG Protein is a Rat Fragment protein, in the 21 to 516 aa range, expressed in HEK 293 cells, with >95%, <0.005 EU/µg endotoxin level.
View Alternative Names
Myelin-associated glycoprotein, 1B236, Brain neuron cytoplasmic protein 3, Sialic acid-binding Ig-like lectin 4a, Siglec-4a, Mag
- Mass Spec
Supplier Data
Mass Spectrometry - Recombinant Rat MAG Protein (AB288812)
Mass determination by ESI-TOF. Predicted MW is 54890.25 Da (+/- 10 Da by ESI-TOF). Observed MW is 54899.65 Da.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Rat MAG Protein (AB288812)
SDS-PAGE analysis of ab288812
- HPLC
Supplier Data
HPLC - Recombinant Rat MAG Protein (AB288812)
HPLC analysis of ab288812
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
This protein acts as an adhesion molecule that contributes to the myelination process. It exists as part of a molecular complex that interacts with other oligodendrocyte and Schwann cell proteins. This interaction is important for nerve regeneration and the expansion of the myelin sheath during development and repair. MAG also assists in signaling between axons and glial cells improving cellular communication and myelin integrity.
Pathways
MAG significantly impacts pathways such as the Nogo receptor which is associated with inhibiting axonal growth and regeneration. MAG interacts with the NOGO protein and other members of the Nogo receptor signaling pathway where it functions to regulate neuronal growth and regeneration. Furthermore MAG's interplay with NOGO receptor components contributes to limiting excessive sprouting of axons balancing growth and stability of the nervous system.
Specifications
Form
Lyophilized
General info
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 (PubMed : 8995428, PubMed : 9298990). 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 (By similarity). 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 (PubMed : 17640868). In cerebellar granule cells the inhibition is mediated primarily via binding to neuronal gangliosides (PubMed : 17640868). In sensory neurons, inhibition of neurite extension depends only partially on RTN4R, RTN4RL2 and gangliosides (PubMed : 19367338). Inhibits axon longitudinal growth (PubMed : 9298990). Inhibits axon outgrowth by binding to RTN4R (By similarity). Preferentially binds to alpha-2,3-linked sialic acid (PubMed : 8995428). Binds ganglioside Gt1b (PubMed : 8995428).
Sequence similarities
Belongs to the immunoglobulin superfamily. SIGLEC (sialic acid binding Ig-like lectin) family.
Post-translational modifications
N-glycosylated.. Phosphorylated on tyrosine residues.. Ubiquitinated, leading to proteasomal degradation.
Target data
Complementary Products
Product promise
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