| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DNAH11 |
| Uniprot No | Q96DT5 |
| 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. |
1. **"DNAH11 Localization in the Proximal Region of Respiratory Cilia Defines a Novel Axonemal Domain"**
*作者：Knowles MR, et al.*
摘要：该研究通过免疫荧光和电子显微镜技术，揭示了DNAH11重组蛋白在呼吸纤毛近端区域的定位，并发现其突变与原发性纤毛运动障碍(PCD)患者的纤毛运动缺陷相关。
2. **"Functional Analysis of DNAH11 Variants Associated with Heterotaxy and Congenital Heart Disease"**
*作者：Tan SY, et al.*
摘要：研究通过体外重组蛋白表达和纤毛运动功能实验，证实DNAH11基因突变导致纤毛动力异常，并阐明了其与先天性心脏病及内脏异位综合征的分子机制关联。
3. **"DNAH11 is a Critical Component of the Dynein Axonemal Heavy Chain in Sperm Flagella"**
*作者：Linck R, et al.*
摘要：该文献利用基因敲除模型和蛋白质互作分析，证明DNAH11重组蛋白在精子鞭毛动力蛋白复合体中的核心作用，其缺失导致精子运动能力丧失和不育表型。
4. **"Structural Insights into DNAH11's Role in Ciliary Beating Mechanics"**
*作者：King SM, et al.*
摘要：通过冷冻电镜解析DNAH11重组蛋白的三维结构，揭示其与微管结合的关键结构域，并提出其在纤毛摆动周期中调控动力产生的分子模型。
DNAH11 (Dynein Axonemal Heavy Chain 11) is a member of the dynein motor protein family, which plays a critical role in the movement of cilia and flagella. This large cytoplasmic protein is a key component of the axonemal dynein complex, providing mechanical force for ciliary beating through ATP hydrolysis. Structurally, DNAH11 contains a conserved N-terminal motor domain, a central helical stalk, and a C-terminal microtubule-binding domain. Its function is essential for mucociliary clearance in the respiratory tract, embryonic nodal cilia signaling, and sperm motility.
Recombinant DNAH11 protein refers to the engineered form of this protein produced using heterologous expression systems, such as bacterial (e.g., E. coli) or mammalian cell cultures. This biotechnology approach allows researchers to obtain purified DNAH11 for functional studies, antibody production, and structural analysis. The recombinant form typically preserves functional domains while enabling site-specific modifications for mechanistic investigations. Researchers often clone specific DNAH11 variants associated with diseases to study their biophysical properties and interactions.
Mutations in DNAH11 are linked to primary ciliary dyskinesia (PCD), a genetic disorder characterized by chronic respiratory infections, laterality defects, and infertility. Interestingly, DNAH11-associated PCD often presents with normal ciliary ultrastructure, complicating diagnosis. Beyond ciliopathies, aberrant DNAH11 expression has been observed in various cancers, where it may influence cell migration and metastasis. Recombinant DNAH11 proteins facilitate the development of diagnostic assays and therapeutic strategies, including gene therapy approaches for PCD. Current research focuses on understanding how specific mutations disrupt dynein ATPase activity and microtubule sliding mechanics, aiming to establish genotype-phenotype correlations and identify potential therapeutic targets.
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