| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GMF |
| Uniprot No | P60983 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-142aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMSESLVVCDVAEDLVEKLRKFRFRKETNNA AIIMKIDKDKRLVVLDEELEGISPDELKDELPERQPRFIVYSYKYQHDDG RVSYPLCFIFSSPVGCKPEQQMMYAGSKNKLVQTAELTKVFEIRNTEDLT EEWLREKLGFFH |
| 预测分子量 | 19 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GMF(Glia Maturation Factor)重组蛋白研究的示例参考文献(文献为模拟示例，非真实存在)：
1. **文献名称**：*"Cloning and Functional Characterization of Recombinant Human GMFβ in Inflammatory Signaling"*
**作者**：Kaplan R. et al.
**摘要**：研究报道了人源GMFβ基因的克隆及在大肠杆菌中的重组表达，证实其通过抑制MAPK通路调控神经胶质细胞的炎症反应，为神经退行性疾病治疗提供靶点。
2. **文献名称**：*"Structural Analysis of Recombinant GMFγ and Its Role in Astrocyte Migration"*
**作者**：Dong L. et al.
**摘要**：通过X射线晶体学解析了重组GMFγ的三维结构，并证明其通过激活Rho GTPase促进星形胶质细胞迁移，提示其在神经损伤修复中的作用。
3. **文献名称**：*"Recombinant GMFβ Attenuates Neuroinflammation in Alzheimer’s Disease Models"*
**作者**：Chen H. et al.
**摘要**：利用HEK293细胞表达重组GMFβ蛋白，发现其在小鼠阿尔茨海默病模型中显著降低Aβ沉积和Tau蛋白过度磷酸化，抑制小胶质细胞过度活化。
4. **文献名称**：*"High-Yield Purification and Functional Validation of GMF Isoforms in Autoimmune Demyelination"*
**作者**：Martinez S. et al.
**摘要**：优化了GMFα和GMFβ重组蛋白的纯化工艺，并在多发性硬化症动物模型中验证其通过调节Th17/Treg平衡减轻脱髓鞘病变。
**提示**：以上为模拟文献，实际引用请通过PubMed、Web of Science等平台检索真实文献(关键词如“recombinant GMF protein”或“GMFβ function”)。
**Background of GMF Recombinant Protein**
Glia Maturation Factor (GMF), first identified in the 1980s, is a highly conserved, intracellular protein predominantly expressed in the central nervous system (CNS). It belongs to the ADF/cofilin superfamily and plays a regulatory role in cellular processes such as glial cell differentiation, immune response modulation, and neuronal survival. Structurally, GMF is a 17-kDa protein encoded by the *GMFG* gene, characterized by its actin-binding domains and involvement in cytoskeletal reorganization.
GMF gained attention due to its dual role in neuroinflammation and neurodegeneration. Studies reveal its involvement in modulating pro-inflammatory signaling pathways, including the inhibition of NF-κB and MAPK cascades, thereby influencing microglial activation and cytokine release. Conversely, under pathological conditions like Alzheimer’s disease, Parkinson’s disease, or multiple sclerosis, aberrant GMF expression correlates with exacerbated neuroinflammation and neuronal damage, suggesting its context-dependent functionality.
The development of recombinant GMF (rGMF) leverages biotechnological platforms, such as *E. coli* or mammalian expression systems, to produce purified, bioactive protein for research and therapeutic exploration. Recombinant technology enables precise control over post-translational modifications, enhancing its stability and functional consistency.
Current applications of rGMF include mechanistic studies of neuroimmune interactions, drug screening for anti-inflammatory agents, and potential therapeutic strategies targeting CNS disorders. Its ability to cross the blood-brain barrier in preclinical models further underscores its translational relevance. However, challenges remain in optimizing delivery methods and understanding its long-term effects. Ongoing research aims to clarify GMF's pleiotropic roles and harness its regulatory properties for innovative treatments in neurology and immunology.
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