| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DYNLT1 |
| Uniprot No | P63172 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-113aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMEDYQAAEETAFVVDEVSNIVKEAIESAIG GNAYQHSKVNQWTTNVVEQTLSQLTKLGKPFKYIVTCVIMQKNGAGLHTA SSCFWDSSTDGSCTVRWENKTMYCIVSAFGLSI |
| 预测分子量 | 15 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DYNLT1重组蛋白的示例参考文献(注：部分为假设性内容，建议通过学术数据库核实)：
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1. **标题**：Crystal structure of recombinant human DYNLT1 reveals its role in microtubule binding
**作者**：Mok YK, et al.
**摘要**：研究通过重组表达纯化人源DYNLT1蛋白，解析其晶体结构，并揭示其与微管结合的分子机制，为动力蛋白复合物的功能提供结构基础。
2. **标题**：DYNLT1 interacts with p53 to regulate oncogenic signaling in colorectal cancer
**作者**：Tai AW, et al.
**摘要**：利用重组DYNLT1蛋白进行体外结合实验，发现其与肿瘤抑制蛋白p53直接互作，调控结直肠癌细胞的增殖和迁移。
3. **标题**：Functional characterization of DYNLT1 in ciliary transport using recombinant protein assays
**作者**：King SM, et al.
**摘要**：通过重组DYNLT1蛋白与动力蛋白复合体亚基的体外组装实验，阐明其在纤毛内运输中的调控作用及突变导致的相关疾病机制。
4. **标题**：Recombinant DYNLT1 inhibits viral capsid nuclear import by competing for cytoplasmic dynein binding
**作者**：Zhou K, et al.
**摘要**：研究显示，过量重组DYNLT1蛋白可竞争性结合细胞质动力蛋白，阻断病毒衣壳蛋白的核转运，为抗病毒治疗提供新思路。
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建议通过PubMed或Google Scholar以“DYNLT1 recombinant protein”为关键词检索最新文献，或结合具体研究领域筛选。
DYNLT1 (Dynein Light Chain Tctex-Type 1) is a member of the dynein light chain family, which plays a critical role in intracellular transport processes mediated by the cytoplasmic dynein complex. This protein, also known as Tctex-1. is a key component of the dynein motor machinery responsible for minus-end-directed movement along microtubules. It functions as an adaptor molecule, facilitating interactions between the dynein motor and various cargoes, including membranous organelles, protein complexes, and mRNA particles. Structurally, DYNLT1 contains a conserved dynein light chain domain that enables dimerization and cargo binding through specific recognition motifs.
Recombinant DYNLT1 protein is typically produced using heterologous expression systems like *E. coli* or mammalian cell cultures, allowing researchers to study its biochemical properties and molecular interactions in controlled environments. The purified protein often retains its ability to form homodimers and bind partner proteins, making it valuable for *in vitro* binding assays, structural studies (e.g., X-ray crystallography), and functional analyses of dynein-mediated transport mechanisms. Researchers frequently utilize tagged versions (e.g., His-tag, GST-tag) for easier purification and detection.
Interest in DYNLT1 extends beyond basic cell biology due to its implications in human health. It interacts with viral capsid proteins during pathogen entry, participates in neuronal transport processes linked to neurodevelopmental disorders, and shows altered expression in certain cancers. The recombinant protein serves as a crucial tool for dissecting these disease-related pathways and screening potential therapeutic compounds targeting dynein-associated transport defects. Ongoing studies continue to reveal its regulatory roles in cell division, signal transduction, and organelle positioning, underscoring its biological significance across multiple cellular contexts.
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