MOG (183-191) peptide- Myelin Oligodentrocyte Glycoprotein peptide 183-191, Mouse
MOG (183-191) FVIVPVLGP
MOG (Mouse Myelin Oligodendrocyte Glycoprotein – UniProtKB – Q61885) is a minor component of the myelin sheath of the CNS (Central Nervous System). This protein plays a role in the maintenance of the myelin sheath and in cell-cell communication. MOG (Myelin oligodendrocyte glycoprotein) is an integral membrane glycoprotein type I of the immunoglobulin family (Ig) found exclusively in mammals with a molecular weight around 26-28 kDa.
MOG 183-191 induces EAE
Multiple sclerosis (MS), an autoimmune disease of the central nervous system (CNS), is characterized by primary demyelination. EAE (experimental autoimmune encephalomyelitis) is the most commonly used experimental model for studying multiple Sclerosis. The MOG (183-191) peptide can be used to induce an immune response and provoke a demyelination of the CNS (Central Nervous System). MOG183-191 can generate specific anti-MOG 183-191 antibodies. This process leads to an experimental autoimmune encephalomyelitis to the host.
|Sequence : FVIVPVLGP- Purity : > 95%|
|MW : 940.18 g / mol (C48H77N9O10)|
|For research use|
|Counter-Ion : TFA Salts (see option TFA removal)|
|Delivery format : Freeze dried in polypropylene 2mL microtubes|
|Other names : Myelin Oligodendrocyte Glicoprotein (183-191)|
|Peptide Solubility Guideline|
|Bulk peptide quantities available|
|Product catalog||Size||Price € HT||Price $ USD|
Clin Immunol. 2004 Apr;111(1):53-60. doi: 10.1016/j.clim.2003.12.012
T cell epitope spreading to myelin oligodendrocyte glycoprotein in HLA-DR4 transgenic mice during experimental autoimmune encephalomyelitis
Epitope spreading has been implicated in the pathogenesis of experimental autoimmune encephalomyelitis (EAE) and human multiple sclerosis (MS). T cell epitope spreading has been demonstrated in rodents for myelin basic protein (MBP) and proteolipid protein (PLP) determinants, but not for myelin oligodendrocyte glycoprotein (MOG), another important myelin antigen. Moreover, the role of human autoimmunity-associated MHC molecules in epitope spreading, including HLA-DR2 and DR4, has not been formally examined. To address these questions, we investigated epitope spreading to MOG determinants in HLA-DR4 (DRB1*0401) transgenic mice during EAE. The data show that upon induction of EAE in HLA-DR4 transgenic mice with the immunodominant HLA-DR4-restricted MOG peptide 97–108 (MOG97–108; TCFFRDHSYQEE), the T cell response diversifies over time to MOG181–200 (core: MOG183–191; FVIVPVLGP) and MBP. The spreading epitope MOG181–200 binds with high affinity to HLA-DRB1*0401 and is presented by human HLA-DRB1*0401+antigen presenting cells. Moreover, this epitope is encephalitogenic in HLA-DRB1*0401 transgenic mice. This study demonstrates intra- and intermolecular epitope spreading to MOG and MBP in “humanized” HLA-DR4 transgenic mice.