| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SVIL |
| Uniprot No | O95425 |
| 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 | 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SVIL(Supervillin)重组蛋白的3篇示例文献，包含名称、作者及摘要概括：
1. **《Recombinant Expression and Functional Analysis of Supervillin in Actin Remodeling》**
- **作者**: Thompson, R. et al.
- **摘要**: 研究通过大肠杆菌系统表达并纯化重组SVIL蛋白，验证其与肌动蛋白的结合能力，揭示其在细胞骨架重组中的调控作用。
2. **《Supervillin Knockdown Impairs Cell Migration: Rescue by Recombinant Protein Expression》**
- **作者**: Garcia, S.M. & Seufferlein, T.
- **摘要**: 利用siRNA敲低SVIL后，细胞迁移能力下降;通过外源性重组SVIL蛋白回补实验，证实其通过调控肌动蛋白聚合促进肿瘤细胞侵袭。
3. **《Structural Characterization of Recombinant Supervillin Using Cryo-EM》**
- **作者**: Li, X. et al.
- **摘要**: 通过冷冻电镜解析重组SVIL蛋白的高分辨率结构，发现其N端结构域对肌动蛋白和膜蛋白的多价结合至关重要，为靶向药物设计提供依据。
*注：以上文献为示例性质，实际研究中建议通过PubMed或Web of Science等平台检索最新文章。*
**Background of SVIL (Supervillin) Recombinant Protein**
SVIL, or Supervillin, is a high-molecular-weight actin-binding protein belonging to the villin/gelsolin family. It is widely expressed in vertebrates and plays critical roles in regulating cytoskeletal dynamics, cell adhesion, and motility. Structurally, SVIL contains multiple functional domains, including actin-binding sites, nuclear localization signals, and membrane-association regions, enabling its interaction with diverse cellular components such as actin filaments, myosin II, and membrane-associated signaling complexes.
The protein is prominently localized at cell membranes, particularly in lamellipodia, filopodia, and invadopodia, where it facilitates cytoskeletal remodeling during processes like cell migration, invasion, and vesicle trafficking. SVIL also interacts with nuclear proteins, suggesting roles in gene regulation and chromatin organization. Dysregulation of SVIL has been implicated in pathological conditions, including cancer metastasis, muscular dystrophies, and immune disorders, highlighting its biomedical relevance.
Recombinant SVIL proteins are engineered *in vitro* using expression systems (e.g., bacterial, mammalian) to produce purified, functional forms for research. These proteins retain key domains for binding partners and enzymatic activities, enabling studies on SVIL's molecular mechanisms. Applications include *in vitro* actin polymerization assays, protein interaction studies, and cellular function assays (e.g., wound healing, invasion). Recombinant SVIL also serves as an antigen for antibody development and a tool for exploring therapeutic strategies targeting cytoskeletal dysregulation.
Overall, SVIL recombinant proteins are vital for dissecting its dual roles in cytoskeletal dynamics and nuclear functions, offering insights into cell biology and disease pathogenesis.
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