![]() ![]() Because functional restoration in demyelinating diseases critically depends on the successful generation of oligodendroglial cells, a therapeutic need that is currently unmet, the regulatory mechanism described here might be of particular interest for identifying suitable drug targets and devising novel therapeutic approaches.įingolimod attenuates splenocyte-induced demyelination in cerebellar slice cultures. Experimental evidence suggests that the inhibitory role of p57kip2 depends on specific interactions with binding proteins such as LIMK-1, CDK2, Mash1, and Hes5 either by controlling their site of action or their activity. In contrast, nuclear accumulation of p57kip2 resulted in blocked oligodendroglial differentiation. Nuclear export of p57kip2 was correlated with promoted myelin expression, higher morphological phenotypes, and enhanced myelination in vitro. We found that subcellular distribution of the p57kip2 protein changed during differentiation of rat, mouse, and human oligodendroglial cells both in vivo and in vitro. The p57kip2 gene encodes one such potent inhibitor of oligodendroglial differentiation and this study sheds light on the underlying mode of action. Increasing evidence points to the existence of several molecular inhibitors that act on these cells and interfere with their cellular maturation. However, the overall remyelination capacity remains inefficient because precursor cells often fail to generate new oligodendrocytes. Partial replacement of lost oligodendrocytes and remyelination can occur as a result of activation and recruitment of resident oligodendroglial precursor cells. Multiple sclerosis is an autoimmune disease of the CNS resulting in degeneration of myelin sheaths and loss of oligodendrocytes, which means that protection and electrical insulation of axons and rapid signal propagation are impaired, leading to axonal damage and permanent disabilities. Maintain at 2-8☌ in undiluted aliquots for up to 1 year after date of receipt. Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like) domain.ĬAUTION: Do not confuse myelin-oligodendrocyte glycoprotein (MOG) with oligodendrocyte-myelin glycoprotein (OMG). SIMILARITY: Belongs to the immunoglobulin superfamily. TISSUE SPECIFICITY: Found exclusively in the CNS, where it is localized on the surface of myelin and oligodendrocyte cytoplasmic membranes.ĭEVELOPMENTAL STAGE: A peak of expression has been observed between postnatal days 15 and 25, coinciding with the period of active myelination. SUBCELLULAR LOCATION: Membrane Multi-pass membrane protein. May be involved in completion and/or maintenance of the myelin sheath and in cell-cell communication. May cross react with human and bovine based on sequence similarity.įUNCTION: Minor component of the myelin sheath. Please refer to the Certificate of Analysis for the lot-specific concentration. The antibody binds to a discontinuous epitope present on the extracellular immunoglobulin V-like domain of MOG. Purified in 0.1 M Tris-Glycine, 0.15 M NaCl, pH 7.4 and 0.05% Sodium AzideĪnti-Myelin Oligodendrocyte Glycoprotein (MOG) Antibody is an antibody against Myelin Oligodendrocyte Glycoprotein (MOG) for use in FC, IC, IH & WB. Consistent with MOG's possible adhesive role in the CNS, a homodimeric form of MOG has not only been observed after isolation from the CNS but has additionally been observed in situ. The developmentally late expression of MOG correlates with the later stages of myelinogenesis, suggesting that MOG has a role in the completion, compaction, and/or maintenance of myelin, further suggesting that MOG has an adhesive function within the CNS. MOG is specifically expressed in the CNS on the outermost lamellae of the myelin sheath as well as the cell body and processes of oligodendrocytes. The amino acid sequence of MOG is highly conserved among animal species (>90%), indicative of an important biological function. MOG is a type I integral membrane protein possessing a single extracellular Ig variable domain (Ig-V) (3, 13, 14). Although the disease-inducing role of MOG has been established, its precise function in the CNS remains obscure. Myelin oligodendrocyte glycoprotein (MOG) is a key CNS-specific autoantigen for primary demyelination in multiple sclerosis. 100% Performance Guaranteed Key Spec Table Species ReactivityĪnti-Myelin Oligodendrocyte Glycoprotein (MOG) Antibody ![]()
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