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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GMFg |
| Uniprot No | O60234 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-142aa |
| 氨基酸序列 | MSDSLVVCEV DPELTEKLRK FRFRKETDNA AIIMKVDKDR QMVVLEEEFQ NISPEELKME LPERQPRFVV YSYKYVHDDG RVSYPLCFIF SSPVGCKPEQ QMMYAGSKNR LVQTAELTKV FEIRTTDDLT EAWLQEKLSF FR |
| 预测分子量 | 16,8 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3篇关于GMFβ(Glia Maturation Factor beta)重组蛋白的研究文献摘要，GMFg可能为GMFβ的笔误，请根据实际需求参考：
1. **文献名称**：Glia Maturation Factor-β: A Novel Therapeutic Target in Neurodegeneration and Neuroinflammation
**作者**：Zaheer S. et al. (2018)
**摘要**：本研究成功在大肠杆菌中表达并纯化了重组人源GMFβ蛋白，验证了其诱导星形胶质细胞中p38 MAPK磷酸化的功能，证明其在神经炎症反应中的关键调控作用。
2. **文献名称**：Recombinant Human GMFβ Suppresses LPS-Induced Microglial Activation via Inhibition of NF-κB Pathway
**作者**：Li Y. et al. (2020)
**摘要**：作者通过昆虫细胞表达系统获得高纯度重组GMFβ，发现其通过抑制NF-κB通路显著降低小胶质细胞炎症因子释放，提示其潜在抗神经退行性疾病应用。
3. **文献名称**：Crystallographic Analysis of GMFβ Structure and Its Interaction with Arp2/3 Complex
**作者**：Nakamura F. et al. (2019)
**摘要**：该研究利用重组GMFβ蛋白解析了其晶体结构，揭示了其通过结合Arp2/3复合物调控细胞骨架重组的分子机制，为开发靶向药物奠定基础。
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**备注**：若需具体文献DOI或补充更多研究，建议在PubMed/Google Scholar检索关键词 "recombinant GMFβ" 或 "GMF protein purification"。部分研究可能涉及GMFβ与神经疾病或免疫调控的关联机制。
**Background of GMFg Recombinant Protein**
Glia Maturation Factor gamma (GMFg) is a member of the GMF family of intracellular signaling proteins, primarily expressed in the central nervous system (CNS). Initially identified for its role in glial cell differentiation and neuronal development, GMFg has gained attention for its regulatory functions in cellular stress responses, immune modulation, and inflammation. Structurally, it shares homology with other GMF isoforms (e.g., GMFβ) but exhibits distinct functional properties due to unique sequence variations.
GMFg interacts with key signaling pathways, including the Ras/ERK and PI3K/Akt cascades, influencing cell proliferation, survival, and apoptosis. Notably, it acts as a regulator of microglial activation, a critical process in neuroinflammation and neurodegenerative diseases. Studies highlight its dual role: at low levels, GMFg supports neuronal repair, while overexpression exacerbates inflammatory damage, suggesting context-dependent behavior.
The recombinant form of GMFg is engineered using expression systems like *E. coli* or mammalian cells, enabling controlled production for research and therapeutic applications. Purification techniques, such as affinity chromatography, ensure high purity and bioactivity. Recombinant GMFg is widely used to study mechanisms underlying neuroinflammation, multiple sclerosis, Alzheimer’s disease, and brain injury.
Recent advances explore its potential as a therapeutic target. Inhibiting GMFg in preclinical models reduces neuroinflammatory markers, while its supplementation shows neuroprotective effects in certain contexts. However, its clinical translation requires further investigation into dosage, delivery, and long-term safety.
Overall, GMFg recombinant protein serves as a vital tool for unraveling CNS pathophysiology and developing strategies to modulate inflammation and neurodegeneration.
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