| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TLN1 |
| Uniprot No | Q9Y490 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 92-399aa |
| 氨基酸序列 | MLDGTVKTIMVDDSKTVTDMLMTICARIGITNHDEYSLVRELMEEKKEEITGTLRKDKTLLRDEKKMEKLKQKLHTDDELNWLDHGRTLREQGVEEHETLLLRRKFFYSDQNVDSRDPVQLNLLYVQARDDILNGSHPVSFDKACEFAGFQCQIQFGPHNEQKHKAGFLDLKDFLPKEYVKQKGERKIFQAHKNCGQMSEIEAKVRYVKLARSLKTYGVSFFLVKEKMKGKNKLVPRLLGITKECVMRVDEKTKEVIQEWNLTNIKRWAASPKSFTLDFGDYQDGYYSVQTTEGEQIAQLIAGYIDII |
| 预测分子量 | 62.8 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TLN1重组蛋白相关的代表性文献(内容基于真实研究概括，部分作者和标题为简化示例)：
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1. **文献名称**: *"Structural Basis of Talin1 Recognition by Vinculin in Cell Adhesion"*
**作者**: Goult BT, et al.
**摘要**: 通过重组TLN1蛋白与Vinculin的共结晶实验，揭示了Talin1的VBS结构域如何被Vinculin识别，阐明了细胞黏附中机械信号传递的结构基础。
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2. **文献名称**: *"Recombinant Talin1 Rod Domain Production and Its Role in Integrin Activation"*
**作者**: Calderwood DA, et al.
**摘要**: 研究利用大肠杆菌表达系统制备重组Talin1杆状结构域，证实其通过结合整合素β亚基的胞内段激活整合素信号通路，促进细胞外基质黏附。
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3. **文献名称**: *"Mechanical Unfolding of Talin1 by Single-Molecule Force Spectroscopy"*
**作者**: Yao M, et al.
**摘要**: 使用重组TLN1蛋白进行单分子力学实验，发现其螺旋结构域在机械力作用下逐步展开，揭示了Talin1作为力学感应蛋白的动态构象变化机制。
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4. **文献名称**: *"Talin1 Knockdown via siRNA and Recombinant Protein Rescue in Cancer Cell Migration Assays"*
**作者**: Monkley SJ, et al.
**摘要**: 通过siRNA敲低TLN1抑制癌细胞迁移，并利用重组TLN1蛋白回补恢复迁移能力，证明其在肿瘤转移中的关键作用。
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**备注**：以上文献标题和作者为简化示例，实际文献可通过PubMed或Google Scholar搜索关键词“Talin1 recombinant”“Talin1 structure”“Talin1 integrin”等获取详细信息。
**Background of TLN1 Recombinant Protein**
Talin-1 (TLN1) is a cytoskeletal protein encoded by the *TLN1* gene, playing a pivotal role in cell adhesion, migration, and mechanotransduction. It acts as a critical linker between integrins—transmembrane receptors mediating cell-extracellular matrix interactions—and the actin cytoskeleton. Structurally, TLN1 contains an N-terminal FERM domain (F3 subdomain) that binds integrin cytoplasmic tails and a C-terminal flexible rod domain that associates with actin filaments. This dual binding capability enables TLN1 to regulate integrin activation, clustering, and downstream signaling, thereby influencing cell adhesion strength, spreading, and motility.
Dysregulation of TLN1 is implicated in pathological processes, including cancer metastasis, thrombosis, and immune disorders. For instance, reduced TLN1 expression correlates with impaired platelet aggregation, while its overexpression in tumors may enhance invasive potential. These associations highlight TLN1 as a potential therapeutic target or biomarker.
Recombinant TLN1 protein is produced using expression systems (e.g., *E. coli*, mammalian cells) to study its biochemical and biophysical properties. Purified TLN1 retains functional domains, enabling *in vitro* investigations such as integrin binding assays, actin polymerization studies, or mechanosensitive signaling experiments. Researchers also utilize TLN1 variants (e.g., truncated forms, mutations) to dissect domain-specific functions or mimic disease-related alterations.
Applications span basic research (e.g., elucidating focal adhesion dynamics) to drug discovery (e.g., screening small molecules targeting integrin-TLN1 interactions). Its recombinant form is essential for structural studies (e.g., cryo-EM, X-ray crystallography) and developing engineered cell models to explore mechanobiology. Overall, TLN1 recombinant protein serves as a vital tool for unraveling cellular mechanics and designing precision therapies.
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