| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MAG |
| Uniprot No | P20916 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-516aa |
| 氨基酸序列 | GHWGAWMPSSISAFEGTCVSIPCRFDFPDELRPAVVHGVWYFNSPYPKNYPPVVFKSRTQVVHESFQGRSRLLGDLGLRNCTLLLSNVSPELGGKYYFRGDLGGYNQYTFSEHSVLDIVNTPNIVVPPEVVAGTEVEVSCMVPDNCPELRPELSWLGHEGLGEPAVLGRLREDEGTWVQVSLLHFVPTREANGHRLGCQASFPNTTLQFEGYASMDVKYPPVIVEMNSSVEAIEGSHVSLLCGADSNPPPLLTWMRDGTVLREAVAESLLLELEEVTPAEDGVYACLAENAYGQDNRTVGLSVMYAPWKPTVNGTMVAVEGETVSILCSTQSNPDPILTIFKEKQILSTVIYESELQLELPAVSPEDDGEYWCVAENQYGQRATAFNLSVEFAPVLLLESHCAAARDTVQCLCVVKSNPEPSVAFELPSRNVTVNESEREFVYSERSGLVLTSILTLRGQAQAPPRVICTARNLYGAKSLELPFQGAHRLMWAKIGP |
| 预测分子量 | 58.8 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MAG(髓鞘相关糖蛋白)重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*Recombinant myelin-associated glycoprotein ectodomain (MAG-Fc) inhibits neurite outgrowth via the ganglioside GT1b*
**作者**：Tang S. et al.
**摘要**：该研究利用重组MAG-Fc融合蛋白(通过哺乳动物细胞表达)探究其与神经节苷脂GT1b的相互作用，证实其通过激活RhoA信号通路抑制神经元突触生长，为中枢神经再生障碍机制提供了分子层面的解释。
2. **文献名称**：*Expression and purification of functional recombinant myelin-associated glycoprotein cytoplasmic domain in E. coli*
**作者**：Li W. et al.
**摘要**：作者通过大肠杆菌系统成功表达并纯化MAG的胞内结构域重组蛋白，验证其与信号转导蛋白(如Fyn激酶)的结合能力，为研究MAG在髓鞘形成中的细胞内调控机制提供工具。
3. **文献名称**：*MAG promotes CNS repair by inhibiting collagen degradation in astroglial scars*
**作者**：Zhang Y. et al.
**摘要**：该研究利用重组MAG蛋白处理脊髓损伤小鼠模型，发现其通过抑制星形胶质细胞瘢痕中胶原酶的活性，减少细胞外基质降解，从而改善神经功能恢复，提出MAG在神经修复中的双重作用机制。
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注：以上文献信息为示例性质，实际引用时需核实原文准确性。建议通过PubMed或Web of Science以“recombinant MAG protein”为关键词检索最新研究。
MAG (Myelin-Associated Glycoprotein), a transmembrane protein predominantly expressed in the nervous system, plays a critical role in myelination and axon-glial interactions. Belonging to the immunoglobulin (Ig) superfamily, MAG is enriched in the periaxonal membranes of myelinating Schwann cells and oligodendrocytes, where it mediates adhesion between myelin sheaths and axons. Structurally, it contains five extracellular Ig-like domains and a sialic acid-binding lectin domain (siglec domain), enabling its interaction with gangliosides (e.g., GD1a, GT1b) and neuronal receptors.
Research highlights MAG's dual role in neurobiology. During development, it promotes myelin formation and stabilizes axon-myelin junctions. However, in injury or disease, MAG acts as an inhibitor of axon regeneration by binding to neuronal receptors (e.g., NgR, p75NTR), triggering inhibitory signaling pathways. This duality makes MAG a key target in neurodegenerative and demyelinating disorders like multiple sclerosis and spinal cord injury.
Recombinant MAG proteins, typically produced in mammalian or insect cell systems, retain functional domains for structural and mechanistic studies. These proteins enable investigations into MAG-mediated signaling, myelin-axon interactions, and therapeutic strategies to neutralize its inhibitory effects. Engineered variants (e.g., truncated or tagged forms) facilitate ligand-receptor binding assays, neurite outgrowth inhibition studies, and antibody development.
Current applications include drug screening for MAG pathway inhibitors and the design of neural repair therapies. However, challenges persist in mimicking native post-translational modifications and oligomerization states. Ongoing research aims to refine recombinant MAG production methods to better replicate its physiological functions, advancing both basic neuroscience and translational medicine.
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