| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DNAL4 |
| Uniprot No | O96015 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-105aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGETEGKKDEADYKRLQTFPLVRHSDMPEE MRVETMELCVTACEKFSNNNESAAKMIKETMDKKFGSSWHVVIGEGFGFE ITHEVKNLLYLYFGGTLAVCVWKCS |
| 预测分子量 | 14 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DNAL4(动力蛋白轻链4)重组蛋白的参考文献示例(内容基于研究领域常见方向，部分信息可能需结合实际文献调整)：
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1. **文献名称**: *Structural insights into the dynein light chain DNAL4 and its interaction with the Bardet-Biedl syndrome protein BBS5*
**作者**: Smith J, et al.
**摘要**: 本研究通过重组表达纯化人源DNAL4蛋白，解析其晶体结构，发现其与BBS5蛋白的相互作用界面，揭示了DNAL4在纤毛运输中的潜在调控机制，为Bardet-Biedl综合征的病理机制提供新见解。
2. **文献名称**: *Recombinant DNAL4 facilitates in vitro analysis of dynein motor complex assembly*
**作者**: Lee S, Kim M.
**摘要**: 报道了一种高效重组表达DNAL4蛋白的方法，并证明其在体外可促进动力蛋白复合体的组装，验证了DNAL4在维持动力蛋白功能完整性中的关键作用。
3. **文献名称**: *Functional characterization of DNAL4 mutations in ciliopathies using recombinant protein models*
**作者**: Garcia-Rua V, et al.
**摘要**: 通过构建DNAL4突变体重组蛋白，发现特定突变导致其与动力蛋白中间链的结合能力丧失，解释了患者纤毛运动缺陷的分子基础。
4. **文献名称**: *DNAL4 as a novel regulator of mitochondrial dynamics: Evidence from recombinant protein-based assays*
**作者**: Zhang L, et al.
**摘要**: 利用重组DNAL4蛋白进行体外结合实验，首次发现其与线粒体分裂蛋白Drp1的相互作用，提示DNAL4可能通过调控线粒体网络影响细胞能量代谢。
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注：以上文献为示例性质，建议通过PubMed或Google Scholar以关键词“DNAL4 recombinant”“Dynein light chain 4”检索真实文献。若研究领域较新，可扩展检索动力蛋白轻链家族(如DYNLL1/DYNLL2)相关研究。
**Background of DNAL4 Recombinant Protein**
DNAL4 (Dynein Axonemal Light Chain 4) is a component of the dynein protein complex, which plays a critical role in the motility and structural organization of cilia and flagella. As part of the axonemal dynein family, DNAL4 contributes to the ATP-dependent movement of microtubules, enabling essential biological processes such as cell locomotion, intracellular transport, and the proper functioning of motile cilia in respiratory tissues, reproductive systems, and embryonic development.
Recombinant DNAL4 protein is produced using genetic engineering techniques, typically through the expression of the *DNAL4* gene in heterologous systems like *E. coli* or mammalian cell cultures. This allows for large-scale production of the purified protein with high consistency, avoiding contaminants often associated with native tissue extraction. The recombinant form retains the functional properties of the native protein, including its ability to interact with other dynein subunits and participate in microtubule sliding mechanisms.
Research on DNAL4 has gained attention due to its association with ciliopathies—disorders caused by defective cilia. Mutations in *DNAL4* or dysregulation of its expression are linked to conditions such as primary ciliary dyskinesia (PCD), characterized by chronic respiratory infections, infertility, and situs inversus. The recombinant protein serves as a vital tool for studying these pathologies, enabling in vitro assays, structural analysis, and the development of therapeutic strategies.
Additionally, DNAL4 recombinant protein is utilized in exploring cilia-related signaling pathways, including those involved in development and tissue homeostasis. Its applications extend to drug screening platforms targeting ciliary dysfunction and regenerative medicine. By providing a controlled and abundant source of the protein, recombinant DNAL4 accelerates both basic research and translational studies aimed at understanding and treating cilia-associated diseases.
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