| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MOG |
| Uniprot No | Q61885 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 29-156aa |
| 氨基酸序列 | GQFRVIGPGYPIRALVGDEAELPCRISPGKNATGMEVGWYRSPFSRVVHLYRNGKDQDAEQAPEYRGRTELLKETISEGKVTLRIQNVRFSDEGGYTCFFRDHSYQEEAAMELKVEDPFYWVNPGVLT |
| 预测分子量 | 16.1 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于MOG重组蛋白的3篇参考文献，包含文献名称、作者及摘要内容概括：
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1. **文献名称**：*Production and characterization of recombinant human MOG for antibody detection in demyelinating diseases*
**作者**：Smith A, et al.
**摘要**：该研究描述了重组人源MOG蛋白(全长及胞外域)的表达与纯化方法，并验证其在多发性硬化症(MS)和视神经脊髓炎谱系疾病(NMOSD)患者血清中的抗体检测效果，强调其在临床诊断中的潜在应用价值。
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2. **文献名称**：*Comparative analysis of MOG isoforms in experimental autoimmune encephalomyelitis*
**作者**：Jones B, et al.
**摘要**：通过比较不同重组MOG蛋白(如MOG 1-125和MOG 35-55肽段)在小鼠实验性自身免疫性脑脊髓炎(EAE)模型中的免疫原性，研究发现全长MOG蛋白更易诱导特异性T细胞反应和脱髓鞘病理，提示其在疾病机制研究中的重要性。
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3. **文献名称**：*Structural and functional insights into the MOG antigen via recombinant protein engineering*
**作者**：Wang C, et al.
**摘要**：利用X射线晶体学和体外实验解析重组MOG蛋白的构象表位，发现其IgG样结构域对抗体结合的关键作用，为开发靶向MOG的自身免疫病治疗策略提供结构基础。
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(注：以上文献信息为基于领域内典型研究的模拟描述，实际引用时需以真实文献为准。)
Myelin oligodendrocyte glycoprotein (MOG) is a minor component of the myelin sheath in the central nervous system (CNS), primarily expressed on the surface of oligodendrocytes and myelin membranes. As a member of the immunoglobulin superfamily, MOG spans the membrane once, with an extracellular immunoglobulin-like domain that is a key target in autoimmune demyelinating disorders. Recombinant MOG protein, produced via genetic engineering in systems like *E. coli* or mammalian cell lines, retains specific antigenic epitopes while eliminating contaminants from native sources. This makes it a critical tool for studying autoimmune responses, particularly in conditions like multiple sclerosis (MS) and MOG antibody-associated disease (MOGAD).
Research using recombinant MOG has advanced our understanding of how autoantibodies against MOG contribute to demyelination. In animal models, such as experimental autoimmune encephalomyelitis (EAE), MOG peptides or recombinant proteins are used to induce autoimmune responses, mimicking aspects of human neuroinflammatory diseases. Clinically, recombinant MOG aids in detecting anti-MOG antibodies via cell-based assays or ELISA, improving diagnostic accuracy for MOGAD—a distinct disorder often misclassified as MS. Its high specificity helps differentiate MOGAD from other demyelinating conditions, guiding personalized treatment strategies.
Therapeutic applications are also emerging. Recombinant MOG is explored in antigen-specific immunotherapies to induce immune tolerance, potentially modulating harmful autoimmune reactions. Additionally, it serves as a substrate for developing monoclonal antibodies or inhibitors targeting pathogenic anti-MOG antibodies. Despite challenges in maintaining native conformational epitopes (especially in prokaryotic expression systems), advancements in protein engineering, such as glycosylation-mimetic modifications in eukaryotic systems, enhance its immunological relevance. Overall, recombinant MOG remains indispensable for unraveling autoimmune mechanisms and bridging translational research in neuroinflammatory diseases.
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