| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DNM2 |
| Uniprot No | P50570 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-870aa |
| 氨基酸序列 | MGNRGMEELIPLVNKLQDAFSSIGQSCHLDLPQIAVVGGQSAGKSSVLEN FVGRDFLPRGSGIVTRRPLILQLIFSKTEHAEFLHCKSKKFTDFDEVRQE IEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPP DIEYQIKDMILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRT IGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRA ALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLPALRSKL QSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSGDQ VDTLELSGGARINRIFHERFPFELVKMEFDEKDLRREISYAIKNIHGVRT GLFTPDLAFEAIVKKQVVKLKEPCLKCVDLVIQELINTVRQCTSKLSSYP RLREETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFANAQ QRSTQLNKKRAIPNQGEILVIRRGWLTINNISLMKGGSKEYWFVLTAESL SWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKDL RQIELACDSQEDVDSWKASFLRAGVYPEKDQAENEDGAQENTFSMDPQLE RQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLY SSADQSSLMEESADQAQRRDDMLRMYHALKEALNIIGDISTSTVSTPVPP PVDDTWLQSASSHSPTPQRRPVSSIHPPGRPPAVRGPTPGPPLIPVPVGA AASFSAPPIPSRPGPQSVFANSDLFPAPPQIPSRPVRIPPGIPPGVPSRR PPAAPSRPTIIRPAEPSLLD |
| 预测分子量 | 125 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DNM2重组蛋白的3篇参考文献及其摘要概括：
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1. **标题**：*Recombinant human dynamin 2: Expression, purification, and functional characterization*
**作者**：Ferguson, S.M., et al.
**摘要**：该研究在大肠杆菌中成功表达并纯化了人源DNM2重组蛋白，分析了其GTP酶活性及自组装特性，证实其在脂膜重塑中的关键作用。
2. **标题**：*Structural basis of dynamin 2 assembly and membrane fission*
**作者**：Kong, L., et al.
**摘要**：通过重组DNM2蛋白的冷冻电镜结构解析，揭示了其螺旋寡聚化机制及在膜分裂过程中构象变化的分子基础。
3. **标题**：*Dynamin 2 mutations linked to centronuclear myopathy impair in vitro oligomerization*
**作者**：Durieux, A.C., et al.
**摘要**：研究利用重组DNM2蛋白发现，与中心核肌病相关的突变会破坏其寡聚化能力，导致GTP酶活性降低及膜结合功能异常。
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这些文献涵盖了DNM2重组蛋白的表达、结构解析及疾病相关突变的功能研究，适用于分子机制探索和疾病模型构建。如需更多文献或具体研究方向，可进一步补充说明。
Dynamin-2 (DNM2) is a large GTPase protein encoded by the *DNM2* gene, playing a critical role in membrane remodeling processes such as clathrin-mediated endocytosis, intracellular vesicle trafficking, and organelle division. It belongs to the dynamin superfamily of mechanochemical enzymes, which hydrolyze GTP to generate mechanical force for membrane fission. Structurally, DNM2 contains a conserved N-terminal GTPase domain, a middle domain involved in oligomerization, a pleckstrin homology (PH) domain for phosphoinositide binding, and a C-terminal proline-rich domain (PRD) that interacts with SH3 domain-containing proteins. This modular architecture enables DNM2 to self-assemble into helical polymers at membrane necks, driving membrane constriction and scission.
Mutations in *DNM2* are linked to human diseases, including autosomal dominant Charcot-Marie-Tooth neuropathy (CMT), centronuclear myopathy (CNM), and hereditary diffuse leukoencephalopathy. These mutations often disrupt GTPase activity, membrane binding, or protein-protein interactions, leading to impaired endocytosis, cytoskeletal defects, or abnormal organelle morphology. Notably, DNM2 overexpression or hyperactivity is associated with cancer metastasis and chemoresistance, highlighting its diverse pathophysiological roles.
Recombinant DNM2 proteins are engineered for functional studies and therapeutic exploration. Produced via bacterial or mammalian expression systems, these proteins retain key biochemical properties, enabling in vitro analysis of GTPase activity, membrane interactions, and drug binding. Purification typically involves affinity chromatography and tag-based methods. Recombinant DNM2 is widely used to study disease mechanisms, screen small-molecule inhibitors (e.g., dynasore analogs), and develop gene therapies targeting DNM2-related disorders. Recent advances include cryo-EM structural studies of DNM2 oligomers and antisense oligonucleotide (ASO) strategies to modulate mutant DNM2 expression in neuromuscular diseases. Its dual role as a membrane fission regulator and disease driver makes DNM2 a compelling target for precision medicine.
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