| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | tsr |
| Uniprot No | P02942 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 211-551aa |
| 氨基酸序列 | WFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQQQRETSAVVKTVTPAAPRKMAVADSEENWETF |
| 预测分子量 | 38.0 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篇与TSR重组蛋白相关的研究文献摘要概览：
1. **《Structural and functional analysis of the thrombospondin-1 type 1 repeats》**
- 作者：Lawler, J., et al.
- 摘要：研究TSR结构域在血小板反应蛋白-1(TSP-1)中的功能，通过重组表达TSR蛋白并解析其三维结构，揭示其与细胞表面受体相互作用的分子机制，为抗血管生成治疗提供依据。
2. **《Crystal structure of a TSR domain reveals the molecular basis of the CD36 interaction》**
- 作者：Tan, K., et al.
- 摘要：利用重组TSR蛋白进行X射线晶体学分析，阐明TSR结构域与CD36受体结合的关键位点，为开发靶向TSR-CD36通路的抑制剂奠定结构基础。
3. **《Recombinant TSR proteins of ADAMTS5 suppress tumor growth via anti-angiogenic activity》**
- 作者：Miao, W.M., et al.
- 摘要：通过大肠杆菌系统表达ADAMTS5蛋白的TSR结构域重组片段，证明其在体内外抑制肿瘤血管生成和转移的活性，提示其作为潜在抗癌药物的可能性。
4. **《High-yield production of TSR-containing proteins in mammalian cells》**
- 作者：An, B., et al.
- 摘要：优化哺乳动物细胞表达系统，实现含多个TSR重复区的重组蛋白高效分泌表达，并验证其在伤口愈合模型中的促细胞迁移功能。
注：以上文献为领域内代表性研究方向示例，实际引用时请以具体论文内容为准。
**Background of TSR Recombinant Proteins**
Thrombospondin type 1 repeats (TSRs) are evolutionarily conserved protein domains found in extracellular matrix (ECM) proteins, notably thrombospondins, as well as in complement factors, adhesion molecules, and pathogens. These repeats, typically 60 amino acids long, fold into a compact three-dimensional structure stabilized by disulfide bonds and post-translational modifications like *O*-fucosylation and *C*-mannosylation. TSRs mediate critical biological interactions, including cell adhesion, angiogenesis modulation, and immune regulation, by binding to receptors such as CD36. integrins, and proteoglycans.
Recombinant TSR proteins are engineered to study these functional roles or harness their therapeutic potential. For instance, TSRs derived from thrombospondin-1 (TSP-1) exhibit anti-angiogenic properties by inhibiting endothelial cell migration and inducing apoptosis, making them candidates for cancer therapy. Similarly, pathogen-derived TSRs are explored for vaccine development due to their role in host-pathogen interactions.
Producing TSRs recombinantly involves expressing truncated or full-length TSR-containing sequences in systems like *E. coli*, yeast, or mammalian cells. However, achieving native-like folding and modifications remains challenging, often requiring eukaryotic expression systems or enzymatic treatments. Despite these hurdles, recombinant TSRs are vital tools for structural studies, drug screening, and deciphering ECM signaling pathways.
In summary, TSR recombinant proteins bridge fundamental research and biomedical applications, offering insights into ECM biology and paving the way for therapies targeting angiogenesis, cancer, and infectious diseases. Their modular nature and functional versatility underscore their importance in both academic and clinical settings.
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