| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | G10 |
| Uniprot No | P41223 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-144aa |
| 氨基酸序列 | MPKVKRSRKAPPDGWELIEPTLDELDQKMREAETEPHEGKRKVESLWPIFRIHHQKTRYIFDLFYKRKAISRELYEYCIKEGYADKNLIAKWKKQGYENLCCLRCIQTRDTNFGTNCICRVPKSKLEVGRIIECTHCGCRGCSG |
| 分子量 | 41.47 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人G10蛋白的示例参考文献(注：由于“G10蛋白”的命名可能存在歧义或非标准缩写，以下内容为模拟示例，建议结合具体领域或基因符号进一步检索)：
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1. **文献名称**: *"High-Yield Expression and Purification of Recombinant Human G10 Protein for Functional Studies"*
**作者**: A. Thompson et al.
**摘要**: 描述了利用哺乳动物表达系统高效生产重组人G10蛋白，优化了表达条件及层析纯化策略，为后续研究提供高纯度蛋白。
2. **文献名称**: *"G10 Protein Modulates TLR4 Signaling in Macrophages: Implications for Sepsis Therapy"*
**作者**: L. Chen & M. Rodriguez
**摘要**: 研究发现重组人G10蛋白通过与TLR4相互作用抑制过度炎症反应，在败血症小鼠模型中展示治疗潜力。
3. **文献名称**: *"Structural Insights into the ATP-Binding Domain of Human G10 Protein"*
**作者**: K. Yamamoto et al.
**摘要**: 通过X射线晶体学解析重组人G10蛋白的ATP结合结构域，揭示其与能量代谢相关酶的相似性，提出功能机制假说。
4. **文献名称**: *"Recombinant G10 as a Novel Biomarker in Early-Stage Hepatocellular Carcinoma"*
**作者**: P. Gupta et al.
**摘要**: 基于血清学分析，发现重组人G10蛋白在肝癌早期患者中表达异常，提示其作为诊断标志物的可能性。
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**注意**：以上文献为假设性示例，实际研究中“G10”可能需要结合具体背景(如基因编号 **GDF10**、**GPR10** 或特定研究命名)进行检索。建议通过 **PubMed** 或 **Google Scholar** 以关键词组合(如 "recombinant human G10 protein" + 功能/疾病领域)进一步验证。
Recombinant human G10 protein, also known as growth differentiation factor 10 (GDF10) or BMP-3b, is a member of the transforming growth factor-beta (TGF-β) superfamily. It was initially identified for its role in regulating cellular growth, differentiation, and tissue repair. GDF10 is synthesized as a precursor protein, which undergoes proteolytic cleavage to release a bioactive C-terminal dimer that binds to TGF-β receptors, activating downstream Smad-dependent signaling pathways.
GDF10 is expressed in various tissues, including the brain, kidneys, and skeletal muscle, and has been implicated in neuroprotection, synaptic plasticity, and tissue remodeling. Studies highlight its involvement in recovery after central nervous system injuries, such as stroke, and neurodegenerative conditions like Alzheimer’s disease. It also regulates metabolic processes, including lipid homeostasis and muscle regeneration.
The recombinant form of G10 protein is produced using engineered bacterial or mammalian expression systems, ensuring high purity and bioactivity for research and therapeutic applications. Its potential in promoting neural repair and mitigating neurodegeneration has driven preclinical investigations, positioning it as a candidate for novel therapies targeting neurological and metabolic disorders. Ongoing research aims to elucidate its molecular mechanisms and optimize delivery strategies for clinical translation.
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