| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TNS1 |
| Uniprot No | Q9HBL0 |
| 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 | 197 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TNS1重组蛋白的3篇参考文献及其摘要内容的模拟示例(注：部分文献信息为假设性内容，实际引用时需核实数据库)：
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1. **文献名称**: *"Functional analysis of recombinant TNS1 in cell migration and adhesion"*
**作者**: Lo SH, et al.
**摘要**: 本研究通过构建TNS1羧基端重组蛋白(包含SH2结构域)，发现其在体外显著抑制成纤维细胞的迁移能力，并证实其与整合素β1的相互作用。重组蛋白的表达揭示了TNS1通过调节黏着斑动态影响细胞运动。
2. **文献名称**: *"Recombinant TNS1 fragments suppress tumor invasion by modulating RhoA signaling"*
**作者**: Sakashita S, et al.
**摘要**: 作者纯化了TNS1的重组PTB结构域蛋白，证明其可通过竞争性结合RhoGAP蛋白DLC1.抑制RhoA活性，从而减少乳腺癌细胞的侵袭性。实验结果为靶向TNS1信号通路治疗转移癌提供了依据。
3. **文献名称**: *"Optimized expression and purification of human TNS1 recombinant protein in E. coli"*
**作者**: Chen H, et al.
**摘要**: 本研究优化了TNS1氨基端重组蛋白(含actin结合域)在大肠杆菌中的可溶性表达条件，采用亲和层析技术获得高纯度蛋白。该重组蛋白成功用于体外肌动蛋白共沉淀实验，验证了其骨架蛋白功能。
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**备注**：上述文献为示例性质，实际研究中建议通过PubMed、Web of Science等平台检索最新文献，并关注TNS1在特定疾病模型(如纤维化、癌症)或信号通路中的重组蛋白应用研究。
TNS1 (Tensin-1) is a multidomain cytoskeletal protein that plays a critical role in regulating cell-matrix adhesion, migration, and signaling. As a member of the tensin family, it localizes to focal adhesion sites, where it interacts with integrins, actin filaments, and signaling molecules to bridge the extracellular matrix (ECM) with intracellular machinery. Structurally, TNS1 contains an N-terminal phosphatase domain, a protein-interacting Src homology 2 (SH2) domain, and a C-terminal actin-binding region, enabling its dual role in mechanical force transmission and signal transduction.
Physiologically, TNS1 is essential for maintaining tissue integrity, wound healing, and embryonic development. Dysregulation of TNS1 has been implicated in pathological conditions, including cancer progression, fibrosis, and cardiovascular diseases. For instance, reduced TNS1 expression correlates with enhanced tumor metastasis, while its overexpression is linked to fibrotic tissue remodeling. These context-dependent roles highlight its therapeutic potential as a biomarker or intervention target.
Recombinant TNS1 protein, produced via heterologous expression systems (e.g., E. coli, mammalian cells), retains functional domains for biochemical and cell-based studies. It enables researchers to explore molecular mechanisms of cell adhesion, screen for drug candidates targeting ECM-related diseases, or engineer biomimetic scaffolds for regenerative medicine. Purified recombinant TNS1 also facilitates structural studies to resolve its domain-specific interactions or post-translational modifications. Despite challenges in maintaining native conformation during production, advances in protein engineering have improved its stability and bioactivity, making it a versatile tool for both basic research and translational applications. Its study continues to uncover novel insights into ECM dynamics and disease pathogenesis.
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