MAG/GMA Antibody [E22A5] | Primary Antibodies

Application: Reactivity: Mouse, Rat, Human

Usage Information

Dilution
WB1:1000 IP1:30 IHC1:2000 IF1:50

Application
WB, IP, IHC, IF

Reactivity
Mouse, Rat, Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
69 kDa 100 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Positive Control	Human cerebellum tissue; Mouse brain tissue; Mouse cerebellum tissue; Rat cerebellum tissue; Mouse hippocampus tissue; Human sciatic nerve tissue; Rat hippocampus tissue; Rat primary neural/glia cell
Negative Control	Rat liver tissue; Mouse liver tissue; Human liver tissue

Datasheet & SDS

Biological Description

Specificity
MAG/GMA Antibody [E22A5] detects endogenous levels of total MAG/GMA protein.

Clone
E22A5

Synonym(s)
GMA; MAG; Myelin-associated glycoprotein; Siglec-4a

Background
MAG, or Myelin-Associated Glycoprotein, is a type I transmembrane sialoadhesin from the immunoglobulin superfamily, expressed by oligodendrocytes and Schwann cells at the innermost adaxonal myelin wrap. It mediates bidirectional glia-axon signaling, maintaining periaxonal spacing (~14 nm) while inhibiting nerve regeneration. The extended rod-like ectodomain comprises five tandem Ig-like domains (Ig1-5, distal to proximal). The Ig1 domain features a β-sandwich with DE and FG loops that bind α2,3-sialylated gangliosides GD1a/LM1 via a hydrophobic pocket formed by Arg118, Gln121, and Trp123, which recognizes terminal sialic acid. A Cys37-Cys165 interdomain disulfide bridge Ig1 and Ig2, while Ig4 and Ig5 facilitate homodimerization at a membrane-proximal ~2-fold symmetry junction. N-linked glycosylation at Asn167 blocks the dimer interface, and Trp27 near the Ig1 ligand site undergoes C-mannosylation. The L-type isoform, predominant in the CNS, has an 89% longer cytoplasmic tail that binds Fyn kinase. MAG’s primary functions include trans-adhesion, where Ig1 engages axonal gangliosides to maintain myelin-axon spacing (with MAG deficiency leading to paranodal disorganization); cis-dimerization via Ig4/Ig5, which rigidifies the periaxonal scaffold and transmits mechanical stability; and inhibitory signaling, where ganglioside binding activates PirB, NgR1, or PlexA4 receptors and downstream RhoA/ROCK pathways, collapsing growth cones and inhibiting neurite outgrowth (structure-guided Ig1 mutants abolish this effect). Reverse signaling through MAG promotes myelination. MAG enforces long-term myelin integrity, as axons degenerate after one year in its absence despite normal initial myelination, structures nodes of Ranvier by clustering Na_v and Caspr, and balances regeneration versus stability as an inhibitor in the adult PNS and CNS. Disease relevance includes anti-MAG IgM gammopathy causing demyelinating neuropathy via the carbohydrate epitope and implications in MS remyelination failure and remodeling defects.

Background

MAG, or Myelin-Associated Glycoprotein, is a type I transmembrane sialoadhesin from the immunoglobulin superfamily, expressed by oligodendrocytes and Schwann cells at the innermost adaxonal myelin wrap. It mediates bidirectional glia-axon signaling, maintaining periaxonal spacing (~14 nm) while inhibiting nerve regeneration. The extended rod-like ectodomain comprises five tandem Ig-like domains (Ig1-5, distal to proximal). The Ig1 domain features a β-sandwich with DE and FG loops that bind α2,3-sialylated gangliosides GD1a/LM1 via a hydrophobic pocket formed by Arg118, Gln121, and Trp123, which recognizes terminal sialic acid. A Cys37-Cys165 interdomain disulfide bridge Ig1 and Ig2, while Ig4 and Ig5 facilitate homodimerization at a membrane-proximal ~2-fold symmetry junction. N-linked glycosylation at Asn167 blocks the dimer interface, and Trp27 near the Ig1 ligand site undergoes C-mannosylation. The L-type isoform, predominant in the CNS, has an 89% longer cytoplasmic tail that binds Fyn kinase. MAG’s primary functions include trans-adhesion, where Ig1 engages axonal gangliosides to maintain myelin-axon spacing (with MAG deficiency leading to paranodal disorganization); cis-dimerization via Ig4/Ig5, which rigidifies the periaxonal scaffold and transmits mechanical stability; and inhibitory signaling, where ganglioside binding activates PirB, NgR1, or PlexA4 receptors and downstream RhoA/ROCK pathways, collapsing growth cones and inhibiting neurite outgrowth (structure-guided Ig1 mutants abolish this effect). Reverse signaling through MAG promotes myelination. MAG enforces long-term myelin integrity, as axons degenerate after one year in its absence despite normal initial myelination, structures nodes of Ranvier by clustering Na_v and Caspr, and balances regeneration versus stability as an inhibitor in the adult PNS and CNS. Disease relevance includes anti-MAG IgM gammopathy causing demyelinating neuropathy via the carbohydrate epitope and implications in MS remyelination failure and remodeling defects.

References
https://pubmed.ncbi.nlm.nih.gov/19156870/ https://pubmed.ncbi.nlm.nih.gov/27922006/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%