| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DNCH1 |
| Uniprot No | Q14204 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-197aa |
| 氨基酸序列 | MISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKRTVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVSDFSERIKQLQNISLAAASGGAKELKVKALLTSLGWSAAVLGWGGSGSGEKHRAQV |
| 分子量 | 48.6 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DYNC1H1(可能为用户所指的DNCH1)蛋白的示例参考文献，包含文献名称、作者及摘要概述：
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1. **文献名称**: *"Recombinant expression and functional characterization of human DYNC1H1 in a baculovirus-insect cell system"*
**作者**: Smith A, et al.
**摘要**: 本研究利用杆状病毒-昆虫细胞系统成功表达并纯化了重组人DYNC1H1蛋白，分析了其ATP酶活性及微管结合能力，为动力蛋白功能研究提供了工具。
2. **文献名称**: *"Structural insights into DYNC1H1 mutations linked to neurological disorders"*
**作者**: Chen L, et al.
**摘要**: 通过重组DYNC1H1蛋白的晶体结构解析，揭示了致病突变如何破坏蛋白构象，影响神经元内运输功能，为相关神经退行性疾病的机制提供了依据。
3. **文献名称**: *"DYNC1H1 interacts with LIS1: A study using recombinant proteins and single-molecule imaging"*
**作者**: Patel R, et al.
**摘要**: 利用重组DYNC1H1与LIS1蛋白的共表达实验，结合单分子成像技术，阐明了二者在胞内物质运输中的协同作用机制。
4. **文献名称**: *"Functional analysis of DYNC1H1 variants in mitotic spindle organization"*
**作者**: Gonzalez M, et al.
**摘要**: 通过重组突变体DYNC1H1的体外实验，发现特定结构域突变导致有丝分裂纺锤体组装异常，提示其在细胞分裂中的关键作用。
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**说明**：上述文献为示例性参考，实际研究需根据具体需求检索权威数据库(如PubMed、Web of Science)。DYNC1H1相关研究多聚焦于神经疾病、细胞分裂及运输机制，重组蛋白技术常用于其功能与互作研究。
Recombinant human DNCH1 protein, derived from the cytoplasmic dynein 1 heavy chain gene (DYNC1H1), is a critical molecular motor involved in microtubule-based intracellular transport. Dynein heavy chains, including DNCH1. form the core structure of the dynein complex, providing ATPase activity and mechanical force generation. The DNCH1 protein contains conserved functional domains, such as the N-terminal stem domain for cargo binding, the AAA+ ATPase modules for energy conversion, and a microtubule-binding stalk. Its role extends to vital cellular processes, including organelle positioning, mitotic spindle organization, and axonal transport in neurons.
Mutations in DYNC1H1 are linked to neurodevelopmental disorders (e.g., malformation of cortical development) and motor neuron diseases due to impaired transport mechanisms. Recombinant DNCH1 is typically produced in heterologous systems like insect or mammalian cells to preserve post-translational modifications and functional integrity. Its applications span in vitro studies of dynein-driven motility, drug screening for neurodegenerative diseases, and structural analysis of microtubule-dynein interactions. Current research focuses on understanding DNCH1's interplay with dynactin and regulatory proteins like LIS1. as well as its dysfunction in cancer metastasis and ciliopathies. The protein’s recombinant form accelerates mechanistic studies while avoiding challenges associated with native dynein purification.
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