| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DST |
| Uniprot No | Q03001 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-195aa |
| 氨基酸序列 | MHSSSYSYRSSDSVFSNTTSTRTSLDSNENLLLVHCGPTLINSCISFGSESFDGHRLEMLQQIANRVQRDSVICEDKLILAGNALQSDSKRLESGVQFQNEAEIAGYILECENLLRQHVIDVQILIDGKYYQADQLVQRVAKLRDEIMALRNECSSVYSKGRILTTEQTKLMISGITQSLNSGFAQTLHPSLTSG |
| 预测分子量 | 23.7 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3篇关于DST(Dystonin)重组蛋白研究的示例参考文献(注：以下内容为模拟示例，非真实文献)：
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1. **文献名称**: *"Functional Analysis of Recombinant DST Isoforms in Epidermal Keratinocytes"*
**作者**: Tanaka K., et al.
**摘要**: 本研究在大肠杆菌中表达了人源DST蛋白的两种重组异构体(DST-A和DST-B)，验证其与中间丝蛋白的结合能力，并发现DST-B在维持角质细胞机械强度中起关键作用，为表皮松解症机制研究提供依据。
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2. **文献名称**: *"Crystal Structure of the DST Actin-Binding Domain and Its Pathogenic Mutations"*
**作者**: Chen L., et al.
**摘要**: 通过X射线衍射解析了DST蛋白的肌动蛋白结合域三维结构，发现p.Arg1256Cys突变导致结构紊乱，解释了该突变引发遗传性感觉神经病变的分子机制。
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3. **文献名称**: *"High-Yield Production of Bioactive DST Protein Using Baculovirus Expression System"*
**作者**: Müller S., et al.
**摘要**: 开发了基于昆虫细胞的重组DST蛋白表达纯化方案，获得高纯度(>95%)、具有微管结合活性的蛋白，为体外药物筛选平台建立提供标准化蛋白来源。
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建议通过PubMed或Web of Science搜索真实文献，关键词可尝试：
"recombinant dystonin"、"DST protein purification"、"dystonin gene therapy"
筛选时注意研究领域(神经退行性疾病/皮肤疾病/细胞骨架研究)。
DST recombinant protein is a engineered biomolecule derived from the DST (Dystonin) gene, which encodes a critical cytoskeletal linker protein belonging to the plakin family. Initially identified for its role in maintaining cellular structural integrity, DST interacts with intermediate filaments, microtubules, and actin networks, facilitating mechanical stability and intracellular organization. Mutations in DST are associated with hereditary disorders like epidermolysis bullosa and neurodegenerative conditions, highlighting its physiological significance.
The development of recombinant DST protein leverages modern biotechnological platforms, such as bacterial, yeast, or mammalian expression systems, to produce purified, functional protein domains. This approach allows researchers to isolate specific isoforms or truncated variants of DST, overcoming challenges posed by its large molecular size (>600 kDa) and complex multidomain structure (e.g., actin-binding domains, plakin repeats). Recombinant technology enables precise control over post-translational modifications, enhancing reproducibility for experimental and therapeutic applications.
In research, DST recombinant proteins serve as tools to study cell adhesion, cytoskeletal dynamics, and neuronal axon guidance mechanisms. They are also employed in drug screening assays targeting DST-related pathologies. Therapeutically, engineered DST variants hold potential for protein replacement therapies or as stabilizing agents in gene-editing strategies for DST-linked diseases. Despite advancements, production hurdles persist, including maintaining native conformational stability and achieving cost-effective scalability. Ongoing optimization of expression systems and purification protocols continues to expand the utility of DST recombinant proteins in both basic science and translational medicine.
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