| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Dyn |
| Uniprot No | O00429 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-736aa |
| 氨基酸序列 | MEALIPVINKLQDVFNTVGADIIQLPQIVVVGTQSSGKSSVLESLVGRDLLPRGTGIVTRRPLILQLVHVSQEDKRKTTGEENGVEAEEWGKFLHTKNKLYTDFDEIRQEIENETERISGNNKGVSPEPIHLKIFSPNVVNLTLVDLPGMTKVPVGDQPKDIELQIRELILRFISNPNSIILAVTAANTDMATSEALKISREVDPDGRRTLAVITKLDLMDAGTDAMDVLMGRVIPVKLGIIGVVNRSQLDINNKKSVTDSIRDEYAFLQKKYPSLANRNGTKYLARTLNRLLMHHIRDCLPELKTRINVLAAQYQSLLNSYGEPVDDKSATLLQLITKFATEYCNTIEGTAKYIETSELCGGARICYIFHETFGRTLESVDPLGGLNTIDILTAIRNATGPRPALFVPEVSFELLVKRQIKRLEEPSLRCVELVHEEMQRIIQHCSNYSTQELLRFPKLHDAIVEVVTCLLRKRLPVTNEMVHNLVAIELAYINTKHPDFADACGLMNNNIEEQRRNRLARELPSAVSRDKSSKVPSALAPASQEPSPAASAEADGKLIQDSRRETKNVASGGGGVGDGVQEPTTGNWRGMLKTSKAEELLAEEKSKPIPIMPASPQKGHAVNLLDVPVPVARKLSAREQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLKALQGASQIIAEIRETHLW |
| 预测分子量 | 81,8 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. |
以下是关于重组动力蛋白(Dynein)的3篇示例参考文献，涵盖表达、功能及结构研究：
1. **《重组人胞质动力蛋白的异源表达与运动特性分析》**
- 作者：Smith A, et al.
- 摘要：通过杆状病毒-昆虫细胞系统成功表达并纯化全长人胞质动力蛋白，验证其微管结合能力及ATP依赖的运动活性，为体外研究马达蛋白机制提供工具。
2. **《重组动力蛋白轻链DYNLL1在神经元囊泡运输中的功能研究》**
- 作者：Chen B, et al.
- 摘要：利用大肠杆菌表达重组DYNLL1蛋白，证实其通过调控动力蛋白复合物参与神经元内逆向运输，缺失导致运输障碍，提示与神经退行性疾病关联。
3. **《冷冻电镜解析重组动力蛋白臂的分子结构》**
- 作者：Johnson R, et al.
- 摘要：通过重组表达动力蛋白马达结构域，结合冷冻电镜技术揭示其ATP水解循环中的构象变化，阐明驱动微管滑动的分子机制。
注：以上文献为示例，实际引用时请核实真实来源及细节。如需具体文献检索，建议使用PubMed或Web of Science等平台。
Dyn recombinant proteins, derived from the dynamin protein family, are engineered to study cellular processes involving membrane remodeling and vesicle trafficking. Dynamins are large GTPases known for their critical role in endocytosis, particularly in severing nascent vesicles from plasma membranes. The dynamin family includes classical dynamins (Dyn1. Dyn2. Dyn3) and dynamin-related proteins (Drp1. OPA1), which regulate mitochondrial fission and fusion. Recombinant dynamin proteins are produced via heterologous expression systems (e.g., E. coli, mammalian cells) to enable biochemical and structural studies.
Interest in dynamin surged in the 1990s when its GTP-dependent mechanochemical activity was linked to membrane scission. Dyn recombinant proteins allow researchers to dissect molecular mechanisms, such as how dynamin oligomerizes into helical structures at membrane necks or interacts with binding partners like endophilin and amphiphysin. Mutant variants (e.g., GTPase-deficient K44A) have been instrumental in probing dynamin's functional domains.
Applications span neuroscience (studying synaptic vesicle recycling), virology (viral entry mechanisms), and drug development. Dysfunctional dynamin is implicated in Charcot-Marie-Tooth disease, mitochondrial disorders, and cancer. Recombinant dynamin also aids in high-throughput screening for pharmacological inhibitors (e.g., dynasore, mito-dynoleptins) targeting membrane trafficking pathways.
Recent advancements include cryo-EM structures of dynamin polymers and optogenetic tools to spatiotemporally control dynamin activity. These innovations, combined with recombinant protein technology, continue to unravel dynamin's role in cellular homeostasis and disease.
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