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Myelin oligodendrocyte glycoprotein (MOG) is a highly conserved, surface-exposed myelin protein and an important autoantigen in neuroimmunology and inflammatory demyelinating disease research. The canonical human MOG isoform contains 247 amino acids, while alternative splicing generates multiple protein isoforms.
This protein hub summarizes key MOG biology, structure and disease relevance and brings together JPT products related to human and mouse MOG, from defined peptide sequences to overlapping and peptide-resolved formats.
MOG Protein: Structure, Localization and Conservation
MOG is a minor component of central nervous system myelin that is expressed on oligodendrocytes and preferentially localized at the outermost surface of the myelin sheath. This exposed position distinguishes MOG from many proteins embedded deeper within compact myelin and makes extracellular regions of the protein accessible to immune recognition.
The canonical reviewed human UniProt sequence contains 247 amino acids and has a calculated mass of approximately 28.2 kDa. UniProt currently annotates 13 isoforms generated by alternative splicing, so protein length and C-terminal composition can differ depending on the isoform being studied.
MOG contains an extracellular immunoglobulin-like domain and is highly conserved across mammalian species. This conservation is biologically relevant, but small sequence differences between species can still be critical for peptide-based experiments and should be considered when selecting mouse or human reagents.
Experimentally determined crystal structures are available for the extracellular MOG domain. High-resolution X-ray structures have shown an Ig-like fold and provide a structural framework for interpreting surface-exposed and conformational epitopes. Examples include PDB entries 1PKO and 1PY9.
Explore JPT MOG Peptides and Related Products
JPT's MOG portfolio includes defined mouse and human antigen sequences as well as broader human MOG formats. The best choice depends primarily on the organism, whether one defined region or broader sequence coverage is required, and whether multiple sequences should be used together or evaluated individually.
MOG in Autoimmunity and Demyelinating Disease Research
The extracellular accessibility of MOG has made it an important autoimmune target in inflammatory disorders of the central nervous system. Autoantibodies against conformational MOG epitopes define MOG antibody-associated disease (MOGAD), an inflammatory demyelinating disease that can present with optic neuritis, myelitis, acute disseminated encephalomyelitis and other CNS syndromes.
MOGAD is now recognized as a disease entity that is biologically and clinically distinct from classical multiple sclerosis and aquaporin-4-positive neuromyelitis optica spectrum disorder. At the same time, MOG has a long history as an experimental autoantigen in multiple-sclerosis and demyelination research, particularly through experimental autoimmune encephalomyelitis models.
This disease relevance explains why different MOG-derived research formats are useful: a project may require one defined linear sequence, broader representation of a protein region, or peptide-resolved comparison across the sequence. JPT provides these formats as distinct catalog products so researchers can select according to organism and experimental question.
Compare JPT Products for MOG Research
MOG Research Resources
This protein hub connects the biological context of MOG with JPT's available catalog products and related scientific resources.
Scientific references
Autoimmune research
Custom peptide synthesis