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MOG (92-106) peptide – Myelin Oligodendrocyte Glycoprotein peptide 92-106, Mouse


MOG (Mouse Myelin oligodendrocyte glycoprotein – UniProtKB – Q61885) is a protein with a molecular weight around 26-28 kDa, located on the external surface of the peripheral lamellae of myelin sheaths of the CNS (Central Nervous System). Myelin oligodendrocyte glycoprotein (MOG) is an integral membrane glycoprotein type I of the immunoglobulin family (Ig) found exclusively in mammals.

MOG 92-106 induces EAE in mouse

This peptide is a fragment of amino acids 92-106 from Myelin oligodendrocyte glycoprotein (MOG). The MOG 92-106 peptide can be used to induce the production of polyclonal anti-MOG 92-106 antibodies. The epitope MOG (92–106) is a DR4-restricted Th cell epitope and a target for demyelinating auto-antibodies. The demyelinating of the myelin sheaths leads to EAE (Experimental Autoimmune Encephalomyelitis) that develops an extensive B cell reactivity against secondary myelin antibodies. MOG can induce Experimental Autoimmune Encephalomyelitis in mouse strain SJL/L like the MOG (35-55) and induces a widespread autoimmune response. The peptide can also induce myelin disease in DA rats and rhesus monkeys.

MOG 92-106 is routinely used in vivo biological evaluation and immunological studies of the Experimental Autoimmune Encephalomyelitis thanks to their high specificity and affinity, they could be used for peptide-coated ELISA and Western-Blot Assay.
The encephalitogenic T cells recognize MOG and some of its immunodominant epitope like MOG (92-106) and induce EAE model that can help to elucidate the immunopathological mechanism of MS (multiple sclerosis).

MOG 92-106

MOG92-106 specifications

PADRE peptide MHC HLA Sequence : DEGGYTCFFRDHSYQ – Purity : > 95%
PADRE peptide adjuvant MW : 1824,88 g / mol (C80H105N21O27S)
PADRE peptide price For research use
PADRE peptide Counter-Ion : TFA Salts (see option TFA removal)
Peptide library synthesis Delivery format : Freeze dried in polypropylene 2mL microtubes
buy synthesized peptides Other names : Myelin Oligodendrocyte Glicoprotein (92-106)
peptide solubility guidelines Peptide Solubility Guideline
buy peptide price Bulk peptide quantities available



Product catalog Size Price € HT Price $ USD
SB139-1MG 1 mg 100 125
SB139-5MG 5 mg 350 435



J Immunol. 2004 Jul 1;173(1):600-6. doi: 10.4049/jimmunol.173.1.600

A Structurally Available Encephalitogenic Epitope of Myelin Oligodendrocyte Glycoprotein Specifically Induces a Diversified Pathogenic Autoimmune Response

Multiple sclerosis is an inflammatory disease of the CNS that involves immune reactivity against myelin oligodendrocyte glyco-protein (MOG), a type I transmembrane protein located at the outer surface of CNS myelin. The epitope MOG92–106 is a DR4-restricted Th cell epitope and a target for demyelinating autoantibodies. In this study, we show that the immune response elicited by immunization with this epitope is qualitatively different from immune responses induced by the well-defined epitopes myelin basic protein (MBP) 84–96 and proteolipid protein (PLP) 139–151. Mice with MOG92–106-, but not with MBP84–96- or PLP139–151-induced experimental autoimmune encephalomyelitis developed extensive B cell reactivity against secondary myelin Ags. These secondary Abs were directed against a set of encephalitogenic peptide Ags derived from MBP and PLP as well as a broad range of epitopes spanning the complete MBP sequence. The observed diversification of the B cell reactivity represents a simultaneous spread toward a broad range of antigenic epitopes and differs markedly from T cell epitope spreading that follows a sequential cascade. The Abs were of the isotypes IgG1 and IgG2b, indicating that endogenously recruited B cells receive help from activated T cells. In sharp contrast, B cell reactivity in MBP84–96- and PLP139–151-induced experimental autoimmune encephalomyelitis was directed against the disease-inducing Ag only. These data provide direct evidence that the nature of the endogenously acquired immune reactivity during organ-specific autoimmunity critically depends on the disease-inducing Ag. They further demonstrate that the epitope MOG92–106 has the specific capacity to induce a widespread autoimmune response. The Journal of Immunology, 2004, 173: 600–606

Autoimmunity . 2008 Nov;41(7):526-36. doi: 10.1080/08916930802128680

Cross-reactive myelin antibody induces renal pathology

 Experimental autoimmune encephalomyelitis (EAE) is an autoimmune model for multiple sclerosis (MS). Previously, we reported renal immunoglobulin (Ig) deposition in mice with myelin oligodendrocyte glycoprotein (MOG(92-106))-induced progressive EAE and naive mice injected with MOG(92-106) hybridoma cells producing antibody that cross-reacts with various autoantigens including double-stranded DNA. To assess whether MOG(92-106) antibodies actually induce kidney changes, the extent of renal Ig deposition and changes in glomerular histology and filtration were investigated. Mice with progressive EAE exhibited Ig deposition, glomerular hypercellularity and proteinuria indicating kidney dysfunction. MOG(92-106) hybridoma cell injected mice also had Ig deposition and proteinuria. Therefore, sensitization with MOG(92-106) and transfer of MOG(92-106) antibodies can induce both central nervous system and renal pathology. The renal involvement reported in MS is believed to occur as a side effect of nephrotoxic drugs or neurogenic bladder. Our results demonstrate that an autoimmune response against myelin could induce pathologic changes in the kidney and may help explain renal changes reported in patients with progressive MS.

Med Chem. 2018 Feb 6;14(2):120-128. doi: 10.2174/1573406413666170906123204.

Myelin Oligodendrocyte Glycoprotein and Multiple Sclerosis

 Myelin oligodendrocyte glycoprotein (MOG) is located on the external surface of myelin, a membranous component of the central nervous system (CNS) that forms the insulating lipid layer around neurons. The major MOG splicing variant (a1 transcript) encodes a transmembrane protein with an extracellular domain of an Ig variable (IgV) fold. MOG IgV domains from the same or different cells dimerize and contribute to the organization and maintenance of the myelin sheath in neurons. The encepalitogenic T cells recognize MOG and its immunodominant epitopes (epitopes 1-22, 35-55 and 92-106 located at the dimer interface) as foreign antigens and cause the destruction of myelin (demyelination) leading to the clinical condition known as multiple sclerosis (MS). Recognition of the antigen takes place in the context of the trimolecular complex formed by HLA, MOGpeptides and TCR.