| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TLN2 |
| Uniprot No | Q9Y4G6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 88-406aa |
| 氨基酸序列 | RPQKIRMLDGSVKTVMVDDSKTVGELLVTICSRIGITNYEEYSLIQETIEEKKEEGTGTLKKDRTLLRDERKMEKLKAKLHTDDDLNWLDHSRTFREQGVDENETLLLRRKFFYSDQNVDSRDPVQLNLLYVQARDDILNGSHPVSFEKACEFGGFQAQIQFGPHVEHKHKPGFLDLKEFLPKEYIKQRGAEKRIFQEHKNCGEMSEIEAKVKYVKLARSLRTYGVSFFLVKEKMKGKNKLVPRLLGITKDSVMRVDEKTKEVLQEWPLTTVKRWAASPKSFTLDFGEYQESYYSVQTTEGEQISQLIAGYIDIILKKK |
| 预测分子量 | 39.1kDa |
| 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TLN2重组蛋白的3篇代表性文献摘要(注：文献信息为模拟示例，非真实存在)：
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1. **文献名称**：*"Expression and purification of recombinant human TLN2 for structural studies"*
**作者**：Chen et al. (2018)
**摘要**：报道了在大肠杆菌中高效表达人源TLN2重组蛋白的方法，通过His标签纯化和凝胶过滤层析获得高纯度蛋白，并利用X射线晶体学初步解析其结构，为TLN2的功能机制研究提供基础。
2. **文献名称**：*"TLN2 regulates cell migration by modulating integrin activation through recombinant protein interaction assays"*
**作者**：Rodriguez & Lee (2020)
**摘要**：通过重组TLN2蛋白与整合素β1亚基的体外结合实验，证明TLN2通过其F3结构域直接激活整合素，并揭示其在调控肿瘤细胞迁移中的关键作用。
3. **文献名称**：*"Functional characterization of TLN2 in mechanotransduction using CRISPR/Cas9 and recombinant protein rescue"*
**作者**：Wang et al. (2021)
**摘要**：结合基因编辑技术和外源添加重组TLN2蛋白，验证了TLN2在细胞机械信号感知中的必要性，发现其缺失导致细胞骨架重塑能力受损，而重组蛋白可部分恢复表型。
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**注**：以上为基于领域知识的模拟文献，实际文献需通过PubMed或Web of Science以关键词“TLN2 recombinant protein”检索获取。
**Background of TLN2 Recombinant Protein**
Talin-2 (TLN2) is a cytoskeletal protein encoded by the *TLN2* gene, playing a critical role in integrin-mediated cell adhesion, migration, and mechanotransduction. As a paralog of Talin-1 (TLN1), TLN2 shares structural similarities, including an N-terminal FERM domain that binds integrin cytoplasmic tails and a C-terminal rod domain that interacts with actin filaments. However, TLN2 exhibits distinct tissue-specific expression patterns, with higher abundance in muscle, brain, and certain epithelial cells, suggesting complementary or specialized functions in these tissues.
TLN2 regulates focal adhesion dynamics by linking integrin receptors to the actin cytoskeleton, thereby modulating cellular responses to extracellular mechanical cues. It also participates in signaling pathways influencing cell survival, proliferation, and tissue morphogenesis. Dysregulation of TLN2 has been implicated in pathologies such as cardiomyopathies, metastatic cancers, and neurological disorders, highlighting its biomedical relevance.
Recombinant TLN2 protein is engineered using expression systems (e.g., *E. coli*, mammalian cells) to produce purified, functional protein for *in vitro* studies. This tool enables researchers to dissect TLN2’s molecular interactions, structural motifs, and role in disease mechanisms. Applications include binding assays, structural analysis (e.g., cryo-EM), and screening for therapeutic compounds targeting integrin-mediated processes. Its production often incorporates tags (e.g., His-tag) for ease of purification and detection.
Overall, TLN2 recombinant protein serves as a vital resource for exploring cell adhesion biology and developing strategies to modulate adhesion-related diseases.
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