Recombinant Human MAG Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-3275

Recombinant Human MAG Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-3275
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Product Overview

Tag His
Host Species Human
Accession P20916
Synonym GMA, S-MAG, SIGLEC-4A, SIGLEC4A
Background The myelin-associated glycoprotein (MAG) contains five immunoglobulin-like domains and belongs to the sialic-acid-binding subgroup of the Ig superfamily. MAG is a transmembrane glycoprotein of 1kDa localized in myelin sheaths of periaxonal Schwann cell and oligodendroglial membranes where it functions in glia-axon interactions. It appears to function both as a receptor for an axonal signal that promotes the differentiation, maintenance and survival of oligodendrocytes and as a ligand for an axonal receptor that is needed for the maintence of myelinated axons. MAG contains a carbohydrate epitope shared with other glycoconjugates that is a target antigen in autoimmune peripheral neuropathy associated with IgM gammopathy and has been implicated in a dying back oligodendrogliopathy in multiple sclerosis. MAG is considered as a transmembrane protein of both CNS and PNS myelin and it strongly inhibits neurite outgrowth in both developing cerebellar and adult dosal root ganglion neurons. In contrast, MAG promotes neurite outgrowth from newborn DRG neurons. Thus, MAG may be responsible for the lack of CNS nerve regeneration and may influce both temporally and spatially regeneration in the PNS.
Description A DNA sequence encoding the human MAG extracellular domain (P20916) (Met 1-Pro 516) was fused with a His tag at the C-terminus.
Source HEK293
Predicted N Terminal Gly 20
AA Sequence Met 1-Pro 516
Molecular Weight The secreted recombinant human MAG comprises 508 a.a. and has a predicted molecular mass of 56 kDa. The apparent molecular mass of rhMAG is approximately 85 kDa in SDS-PAGE under reducing conditions due to glycosylation.
Purity >95% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity 1. Measured by its ability to bind mouse RTN4R-Fc2h in functional Elisa.2. Measured by its ability to bind human RTN4R-Fch in functional Elisa.
Formulation Lyophilized from sterile PBS, pH 7.4.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target 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.
Subcellular Location Cell membrane; Single-pass type I membrane protein. Membrane raft.
Protein Families Immunoglobulin superfamily, SIGLEC (sialic acid binding Ig-like lectin) family
Database References
Associated Diseases Spastic paraplegia 75, autosomal recessive (SPG75)
Tissue Specificity Both isoform 1 and isoform 2 are detected in myelinated structures in the central and peripheral nervous system, in periaxonal myelin and at Schmidt-Lanterman incisures. Detected in optic nerve, in oligodendroglia and in periaxonal myelin sheaths. Detecte

Gene Functions References

  1. we observed two-way correlations between the MOG and MAG levels and the fractional anisotropy and mean diffusivity values in the white matter of the left middle frontal lobe, right inferior parietal lobe, and right supplementary motor area in major depressive disorder patients PMID: 29477585
  2. polyneuropathy associated with anti-MAG antibodies is less homogeneous. PMID: 26065001
  3. This study identify involvement of myelin-associated glycoprotein in this family with a disorder affecting the central and peripheral nervous system, and suggest that loss of the protein function is responsible for the unique clinical phenotype PMID: 26179919
  4. Results show that MAG is important for axon-glia contact in a model for Charcot-Marie-Tooth disease type 1A, and suggest that its increased expression in patients has a compensatory role in the disease pathology PMID: 22940629
  5. Increased serum levels of MAG (and MBP) were found in autistic patients with allergic manifestations compared to those without these manifestations. PMID: 23726766
  6. Primary mitochondrial respiratory chain defects affecting the white matter, and unrelated to inflammation, are associated with MAG loss and central nervous system demyelination. PMID: 22491194
  7. Distal acquired demyelinating symmetric neuropathy without anti-MAG antibodies is more likely to be considered a variant of chronic inflammatory demyelinating polyradiculoneuropathy, including a hematological or immunological condition. PMID: 21199182
  8. polysialylated NCAM persistence, up-regulated polysialyltransferase-1 mRNA and previously uncovered defective myelin-associated glycoprotein may be early pathogenetic events in adult-onset autosomal-dominant leukodystrophy PMID: 19725832
  9. Myelin destruction with preferential loss of MAG is found in autopsy brains with acute white matter ischemia as well as in HSV- and CMV-encephalitis. PMID: 12528815
  10. Possible association of MAG and schizophrenia in a Chinese Han cohort of family trios PMID: 15820319
  11. Our findings of a significant associations between schizophrenia and the MAG gene suggest that this gene may be involved in susceptibility to schizophrenia in the Chinese Han population. PMID: 16039057
  12. Expression of MAG, CNP and OLIG2 did not differ between patients with schizophrenia and controls in the grey or white matter PMID: 17964117
  13. These results support the hypothesis that the adhesive interactions between MUC1 and MAG are of biological significance in pancreatic cancer perineural invasion. PMID: 17974963
  14. Twenty of 46 patients with IgM amyloidosis (7 with and 13 without polyneuropathy) had elevation of anti-MAG or SGPG by enzyme-linked immunosorbent assay PMID: 18236455
  15. This finding provides support for potential association of the CNP gene but not the MAG gene in schizophrenia in a Caucasian population. PMID: 18496213
  16. In our patient, propriospinal myoclonus was associated with anti-MAG polyneuropathy, but the causal relationship remains unclear. PMID: 18816614
  17. RNF10 is a trans-acting protein regulating MAG expression and is required for myelin formation. PMID: 18941509
  18. Taken together, these findings suggest that in anti-MAG neuropathy patients, IgM deposits are entrapped within cutaneous perineurium-ensheathed nerve bundles where they accumulate in the endoneurial space. PMID: 19151627
  19. ELISA is more sensitive than Western blot to diagnose anti-myelin-associated glycoprotein related polyneuropathy, although a positive serology may be found in other forms of polyneuropathy as well. PMID: 19720975

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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