Myelin Oligodendrocyte Glycoprotein (MOG) is a glycoprotein believed to be important in the process of myelinization of nerves in the central nervous system (CNS). It is a transmembrane protein expressed on the surface of oligodendrocyte cell and on the outermost surface of myelin sheaths.
CAT No: 10-101-57
CAS No:163913-87-9
Synonyms/Alias:PMG-3660-PI;MOG (Rat, Mouse, 35-55);163913-87-9;H-Met-Glu-Val-Gly-Trp-Tyr-Arg-Ser-Pro-Phe-Ser-Arg-Val-Val-His-Leu-Tyr-Ar g-Asn-Gly-Lys-OH; Myelin Oligodendrocyte Protein (35-55); MOG (35-55); MEVGWYRSPFSRVVHLYRNGK;
MOG (35-55) peptide, also known as Myelin Oligodendrocyte Glycoprotein (35-55), is a synthetic peptide fragment corresponding to amino acids 35 to 55 of the full-length MOG protein. This compound is widely utilized in neuroscience and immunology research due to its ability to mimic specific epitopes of the native protein, facilitating the study of autoimmune responses and demyelination processes. As a well-characterized antigenic sequence, MOG (35-55) is highly valued for its reproducibility and consistency in experimental models, particularly those investigating the molecular and cellular mechanisms underlying central nervous system disorders. Its synthetic origin ensures batch-to-batch uniformity, making it a reliable reagent for both in vitro and in vivo studies. Researchers appreciate the structural fidelity of this peptide, which allows for precise interrogation of immune cell interactions and the elucidation of pathogenic pathways in neurological research.
Autoimmune Disease Modeling: MOG (35-55) is extensively employed in the induction of experimental autoimmune encephalomyelitis (EAE), an established animal model for studying the pathogenesis of multiple sclerosis and related demyelinating diseases. By administering the peptide to laboratory animals, researchers can reliably trigger immune-mediated demyelination and inflammation within the central nervous system, thereby replicating key aspects of human disease. This approach enables the dissection of immunological events such as T cell activation, cytokine production, and blood-brain barrier disruption, providing insights into disease initiation and progression that are critical for the development of novel therapeutic strategies.
T Cell Epitope Mapping: The use of Myelin Oligodendrocyte Glycoprotein (35-55) in epitope mapping studies helps delineate the specific regions of the MOG protein recognized by pathogenic T cells. By exposing immune cells to the peptide in vitro, investigators can identify and characterize the dominant T cell epitopes involved in autoimmune responses. This information is instrumental in understanding the molecular basis of antigen recognition and immune specificity, as well as in the design of targeted immunomodulatory interventions. The ability to map T cell epitopes with high precision using this peptide advances both basic immunological research and translational efforts aimed at modulating autoreactive lymphocytes.
Neuroinflammation Research: MOG (35-55) serves as a critical tool in the investigation of neuroinflammatory mechanisms associated with demyelinating diseases. By facilitating controlled induction of neuroinflammation in animal models, the peptide enables researchers to monitor the recruitment and activation of various immune cell populations within the central nervous system. This experimental framework supports the evaluation of inflammatory mediators, glial cell responses, and the interplay between innate and adaptive immunity. The insights gained from such studies contribute to a deeper understanding of the cellular and molecular drivers of neuroinflammation, informing the development of anti-inflammatory therapies.
Antigen Presentation Studies: The synthetic MOG peptide is frequently utilized to study antigen processing and presentation by major histocompatibility complex (MHC) molecules on antigen-presenting cells. By incorporating it into cell culture or animal models, researchers can assess how dendritic cells, macrophages, and other antigen-presenting cells process and present the peptide to T lymphocytes. These experiments shed light on the efficiency and specificity of antigen presentation, the activation thresholds of T cells, and the factors that influence immune tolerance versus autoimmunity. Such findings are fundamental to immunological research focused on the regulation of immune responses in the context of central nervous system antigens.
Drug Discovery and Therapeutic Screening: MOG (35-55) is widely used in preclinical drug discovery efforts aimed at identifying compounds that modulate immune responses or prevent demyelination. By incorporating the peptide into screening assays, researchers can evaluate the efficacy of candidate molecules in altering disease phenotypes, suppressing pathogenic immune activity, or promoting remyelination. These applications support the identification of promising therapeutic agents and the elucidation of their mechanisms of action in relevant biological systems. Through its utility in drug screening platforms, the peptide accelerates the translation of basic scientific discoveries into potential treatments for autoimmune and neurodegenerative disorders.
The use of HLA class II-transgenic (Tg) mice has facilitated identification of antigenic T cell epitopes that may contribute to inflammation in T cell-mediated diseases such as rheumatoid arthritis and multiple sclerosis (MS). In this study, we compared the encephalitogenic activity of three DR2-restricted myelin determinants [mouse (m) myelin oligodendrocyte glycoprotein (MOG)-35-55, human (h)MOG-35-55 and myelin basic protein (MBP)-87-99] in Tg mice expressing the MS-associated DR2 allele, DRB1*1501. We found that mMOG-35-55 peptide was strongly immunogenic and induced moderately severe chronic experimental autoimmune encephalomyelitis (EAE) with white matter lesions after a single injection in Freund's complete adjuvant followed by pertussis toxin. hMOG-35-55 peptide,which differs from mMOG-35-55 peptide by a proline for serine substitution at position 42, was also immunogenic, but not encephalitogenic, and was only partially cross-reactive with mMOG-35-55. In contrast, MBP-87-99, which can induce EAE in double-Tg mice expressing both HLA-DR2 and a human MBP-specific TCR, was completely non-encephalitogenic in HLA-DR2-Tg mice lacking the human TCR transgene. These findings demonstrate potent encephalitogenic activity of the mMOG-35-55 peptide in association with HLA-DR2, thus providing a strong rationale for further study of hMOG-35-55 peptide as a potential pathogenic determinant in humans.
Rich, C., Link, J. M., Zamora, A., Jacobsen, H., Meza‐Romero, R., Offner, H., ... & Vandenbark, A. A. (2004). Myelin oligodendrocyte glycoprotein‐35–55 peptide induces severe chronic experimental autoimmune encephalomyelitis in HLA‐DR2‐transgenic mice. European journal of immunology, 34(5), 1251-1261.
Intravenous (i.v.) administration of encephalitogenic peptide can effectively prevent experimental autoimmune encephalomyelitis (EAE), an animal model of multiple sclerosis; however, the underlying cellular and molecular mechanisms are not fully understood. In this study, we induced i.v. tolerance to EAE by administration of MOG(35-55) peptide and determined the effect of this approach on intracellular signaling pathways of the IL-23/IL-17 system, which is essential for the pathogenesis of MS/EAE. In tolerized mice, phosphorylation of JAK/STAT-1, -4, ERK1/2 and NF-kappaBp65 were significantly reduced in splenocytes and the central nervous system. MOG i.v. treatment led to significantly lower production of IL-17, and administration of exogenous IL-17 slightly broke immune tolerance, which was associated with reduced activation of STAT4 and NF-kappaB. Suppressed phosphorylation of these pathway molecules was primarily evident in CD11b(+) and small numbers of CD4(+), CD8(+) and CD11c(+) cells. More importantly, adoptive transfer of CD11b(+) splenocytes of tolerized mice effectively delayed onset and reduced clinical severity of actively induced EAE. This study correlates MOG i.v. tolerance with modulation of Jak/STAT signaling pathways and investigates novel therapeutic avenues for the treatment of EAE/MS.
Jiang, Z., Li, H., Fitzgerald, D. C., Zhang, G. X., & Rostami, A. (2009). MOG35–55 iv suppresses experimental autoimmune encephalomyelitis partially through modulation of Th17 and JAK/STAT pathways. European journal of immunology, 39(3), 789-799.
3. Myotropic activity of allatostatins in tenebrionid beetles
4. Adipose tissue is a key organ for the beneficial effects of GLP-2 metabolic function
If you have any peptide synthesis requirement in mind, please do not hesitate to contact us at . We will endeavor to provide highly satisfying products and services.
Creative Peptides is a trusted CDMO partner specializing in high-quality peptide synthesis, conjugation, and manufacturing under strict cGMP compliance. With advanced technology platforms and a team of experienced scientists, we deliver tailored peptide solutions to support drug discovery, clinical development, and cosmetic innovation worldwide.
From custom peptide synthesis to complex peptide-drug conjugates, we provide flexible, end-to-end services designed to accelerate timelines and ensure regulatory excellence. Our commitment to quality, reliability, and innovation has made us a preferred partner across the pharmaceutical, biotechnology, and personal care industries.
Read More