| 纯度 | ＞80%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TWF1 |
| Uniprot No | Q12792 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 100-350aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHM MLYAA TRATLKKEFG GGHIKDEVFG TVKEDVSLHG YKKYLLSQSS PAPLTAAEEE LRQIKINEVQ TDVGVDTKHQ TLQGVAFPIS REAFQALEKL NNRQLNYVQL EIDIKNEIII LANTTNTELK DLPKRIPKDS ARYHFFLYKH SHEGDYLESI VFIYSMPGYT CSIRERMLYS SCKSRLLEIV ERQLQMDVIR KIEIDNGDEL TADFLYEEVH PKQHAHKQSF AKPKGPAGKR GIRRLIRGPA ETEATTD |
| 预测分子量 | 32 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TWF1(Twinfilin-1)重组蛋白研究的虚构参考文献示例(注意：以下内容为模拟生成，实际文献需通过学术数据库查询)：
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1. **文献名称**：*"Expression and Functional Characterization of Recombinant TWF1 in Cancer Cell Motility"*
**作者**：Chen L. et al.
**摘要**：研究通过大肠杆菌系统表达并纯化了重组人TWF1蛋白，验证了其与肌动蛋白结合的活性，并发现TWF1的缺失显著抑制了乳腺癌细胞的迁移能力，提示其在肿瘤转移中的作用机制。
2. **文献名称**：*"Structural Insights into TWF1-Actin Interaction via Recombinant Protein Crystallography"*
**作者**：Wang Y. et al.
**摘要**：利用昆虫细胞表达系统获得高纯度TWF1重组蛋白，通过X射线晶体学解析了TWF1与肌动蛋白的复合物结构，揭示了其N端结构域在调控细胞骨架动态中的关键作用。
3. **文献名称**：*"TWF1 Recombinant Protein as a Potential Biomarker in Neurodegenerative Diseases"*
**作者**：Rodriguez S. et al.
**摘要**：通过哺乳动物细胞表达重组TWF1蛋白，发现其在阿尔茨海默病模型小鼠脑脊液中表达异常，并与tau蛋白异常聚集相关，为神经退行性疾病诊断提供了新方向。
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如需真实文献，建议通过PubMed、Google Scholar等平台检索“TWF1 recombinant protein”或“Twinfilin-1 expression”等关键词。
TWF1 (Twinfilin-1), a member of the ADF/cofilin protein family, is a conserved actin-binding protein critical for regulating cytoskeletal dynamics. It contains two actin-depolymerizing factor (ADF)-homology domains, enabling its interaction with both monomeric (G-actin) and filamentous actin (F-actin). TWF1 modulates actin polymerization by sequestering G-actin and capping filament barbed ends, thereby balancing actin assembly-disassembly cycles essential for cell motility, morphogenesis, and endocytosis. Its activity is tightly regulated by phosphorylation and interactions with signaling molecules like PIP2 and Rho GTPases.
Recombinant TWF1 proteins are engineered to study its structural and functional properties. Typically produced in *E. coli* or eukaryotic expression systems, these proteins retain biochemical activity while enabling controlled experimental conditions. Tags such as His-tag or GST are often fused to facilitate purification and detection. Recombinant TWF1 has been instrumental in elucidating its role in diseases; for example, dysregulated TWF1 expression correlates with cancer metastasis, immune disorders, and neurological defects. It also serves as a tool for drug screening targeting cytoskeleton-related pathologies.
Recent studies highlight TWF1's involvement in mechanotransduction and cellular stress responses, expanding its relevance beyond basic cytoskeletal regulation. The development of phosphorylation-mimetic mutants (e.g., Ser/Thr to Asp substitutions) has further advanced understanding of post-translational regulation. As actin dynamics gain attention in therapeutic strategies, recombinant TWF1 remains a key reagent for dissecting pathological mechanisms and developing precision interventions.
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