| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DYNC1H1 |
| Uniprot No | Q14204 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 全长 |
| 氨基酸序列 | full |
| 预测分子量 | 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DYNC1H1重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*DYNC1H1 mutations associated with neurological diseases disrupt processive movement of human cytoplasmic dynein in vivo*
**作者**：Willemsen MH, Vissers LEL, Willemsen MAAP, et al.
**摘要概括**：该研究通过表达重组DYNC1H1蛋白，结合活细胞成像技术，揭示了DYNC1H1基因突变如何破坏细胞质动力蛋白的持续性运动能力，从而导致神经发育障碍(如Charcot-Marie-Tooth病)的分子机制。
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2. **文献名称**：*Crystal structure of the dynein motor domain bound to the cytoplasmic dynein heavy chain 1 (DYNC1H1)*
**作者**：Carter AP, Cho C, Jin L, Vale RD
**摘要概括**：本研究利用重组DYNC1H1蛋白解析了动力蛋白核心马达结构域的晶体结构，阐明了其与微管结合及ATP水解的构象变化机制，为理解DYNC1H1在细胞内运输中的作用提供结构基础。
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3. **文献名称**：*Functional characterization of DYNC1H1 variants in neurodevelopmental disorders using recombinant protein models*
**作者**：Hoang HT, Schlager MA, Bullock SL, et al.
**摘要概括**：通过构建DYNC1H1重组蛋白突变体，结合体外微管滑动实验，作者发现特定突变会显著降低动力蛋白的ATP酶活性及运动功能，解释了DYNC1H1突变导致智力障碍和脑畸形的病理机制。
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(注：上述文献信息为示例性质，具体发表年份及作者需根据实际数据库检索结果调整。)
DYNC1H1 is a critical component of the cytoplasmic dynein complex, a multisubunit motor protein responsible for minus-end-directed microtubule-based transport in eukaryotic cells. Encoded by the *DYNC1H1* gene, this heavy chain protein serves as the core ATPase that generates mechanical force for intracellular cargo trafficking, organelle positioning, and mitotic spindle organization. As the largest subunit of the dynein-1 complex, DYNC1H1 contains a conserved motor domain with six AAA+ ATPase modules, a microtubule-binding stalk, and a cargo-binding tail region. Its function is essential for neuronal development, as it mediates retrograde axonal transport of vesicles, signaling molecules, and organelles in neurons.
Recombinant DYNCC1H1 proteins are engineered to study dynein’s mechanochemical properties, interactions with dynactin adaptors (e.g., BICD2), and regulatory mechanisms. These proteins are typically expressed in heterologous systems (e.g., insect or mammalian cells) to preserve post-translational modifications and structural integrity. Researchers utilize purified DYNC1H1 variants to investigate pathogenic mutations linked to neurodevelopmental disorders such as spinal muscular atrophy with lower extremity predominance (SMA-LED), Charcot-Marie-Tooth disease, and malformations of cortical development. In vitro assays with recombinant DYNC1H1 enable analysis of microtubule-binding kinetics, ATP hydrolysis rates, and force generation using optical tweezers or TIRF microscopy. Additionally, they aid in screening therapeutic compounds targeting dynein dysfunction. The protein’s modular architecture allows domain-specific studies, particularly focusing on mutations clustered in the motor and dimerization domains that impair cargo binding or force coupling. By reconciling structural data with cellular phenotypes, DYNC1H1 recombinant tools advance our understanding of intracellular transport mechanisms and their pathophysiological disruptions.
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