| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DNM1 |
| Uniprot No | Q05193 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-245aa |
| 氨基酸序列 | GNRGMEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNATTEYAEFLHCKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSDLANSDALKVAKEVDPQGQRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIDGK |
| 预测分子量 | 28.7 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DNM1重组蛋白的3篇参考文献摘要，供参考：
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1. **文献名称**：*Structural insights into the mechanism of dynamin 1 assembly*
**作者**：Faelber, K. et al.
**摘要**：通过X射线晶体学解析了重组表达的人源DNM1蛋白的寡聚体结构，揭示了其螺旋组装机制，阐明了DNM1在膜分裂中的分子基础。
2. **文献名称**：*Recombinant production and characterization of human dynamin 1 for functional studies*
**作者**：Chappie, J.S. et al.
**摘要**：报道了在大肠杆菌中高效表达并纯化功能性DNM1重组蛋白的方法，验证了其GTP酶活性及与微管结合的能力，为体外功能研究提供技术基础。
3. **文献名称**：*Dynamin 1 mutations associated with neurological disorders alter oligomerization*
**作者**：Kenniston, J.A.H. et al.
**摘要**：利用重组DNM1蛋白突变体研究致病性变异的分子机制，发现突变导致寡聚化异常，影响突触囊泡循环，提示与癫痫等疾病的病理关联。
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注：以上文献为示例，实际引用时请核对期刊名称、年份及具体作者信息。如需最新研究，建议在PubMed或Web of Science检索关键词“DNM1 recombinant”或“dynamin 1 expression”。
**Background of DNM1 Recombinant Protein**
Dynamin-1 (DNM1) is a member of the dynamin family of large GTPases, essential for membrane remodeling processes such as clathrin-mediated endocytosis and mitochondrial fission. It plays a critical role in synaptic vesicle recycling by mediating the scission of vesicles from the plasma membrane. Structurally, DNM1 contains a GTPase domain, a middle domain involved in self-assembly, and a C-terminal pleckstrin homology (PH) domain that binds membrane lipids.
Recombinant DNM1 protein is produced through heterologous expression systems (e.g., *E. coli* or mammalian cell lines) to study its biochemical properties, interactions, and functional mechanisms *in vitro*. This engineered protein retains the ability to hydrolyze GTP and self-assemble into helical polymers, mimicking its native behavior. Researchers utilize DNM1 recombinant protein to investigate its role in membrane dynamics, neuronal signaling, and pathologies linked to dynamin dysfunction, such as epilepsy and neurodevelopmental disorders.
DNM1 mutations are associated with severe epileptic encephalopathies, highlighting its importance in neuronal health. Recombinant DNM1 variants (e.g., pathogenic mutants like p.Arg237Trp) are used to model disease mechanisms and screen potential therapeutic agents. Additionally, studies on DNM1’s interaction with binding partners (e.g., endophilin, amphiphysin) provide insights into regulatory pathways of membrane trafficking.
Overall, DNM1 recombinant protein serves as a vital tool for dissecting the molecular basis of dynamin-dependent processes and advancing therapeutic strategies for related disorders.
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