| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VCL |
| Uniprot No | P18206 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-235aa |
| 氨基酸序列 | PVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVAAVQAAVSNLVRVGKETVQTTEDQILKRDMPPAFIKVENACTKLVQAAQMLQSDPYSVPARDYLIDGSRGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMAKMIDERQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNSKNQGIEEALKNRNFTVE |
| 预测分子量 | 53.0kDa |
| 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VCL(Vinculin)重组蛋白的3篇参考文献示例(注：文献为假设性示例，实际引用需核实)：
1. **文献名称**：*Expression and Functional Characterization of Recombinant Vinculin in Mammalian Cells*
**作者**：Smith J, et al.
**摘要**：研究报道了在哺乳动物细胞中成功表达重组Vinculin蛋白，并验证其通过促进黏着斑形成增强细胞-基质黏附的功能，为研究细胞力学信号传导提供工具。
2. **文献名称**：*Structural Insights into Vinculin Activation Using Engineered Recombinant Fragments*
**作者**：Li H, Wang Y.
**摘要**：通过构建重组Vinculin片段(如Vd1和Vh1)，结合晶体学分析揭示Vinculin自抑制构象的分子机制，阐明其受张力激活的结构基础。
3. **文献名称**：*Recombinant Vinculin-Tagged Nanoparticles for Targeting Focal Adhesions in Cancer Therapy*
**作者**：Garcia R, et al.
**摘要**：开发了重组Vinculin偶联的靶向纳米颗粒，可特异性识别肿瘤细胞黏着斑，增强药物递送效率，为癌症靶向治疗提供新策略。
(若需更多文献方向，可补充说明具体研究领域，如蛋白纯化、结构生物学或疾病应用等。)
**Background of VCL Recombinant Protein**
Vinculin (VCL) is a cytoskeletal protein critical for cell adhesion, migration, and mechanotransduction. It acts as a scaffold, linking integrin-based adhesion complexes to the actin cytoskeleton, thereby stabilizing cell-matrix and cell-cell junctions. Structurally, vinculin consists of a head domain that binds talin and α-catenin, and a tail domain that interacts with actin and other cytoskeletal regulators. Its conformational regulation—switching between inactive (auto-inhibited) and active states—is central to its role in sensing and transmitting mechanical signals.
Recombinant vinculin protein (VCL) is engineered using genetic cloning techniques, typically expressed in bacterial (e.g., *E. coli*) or mammalian systems to ensure proper folding and post-translational modifications. The recombinant form retains functional domains, enabling studies on its interactions, structural dynamics, and role in cellular processes. Purification methods, such as affinity chromatography, yield high-purity VCL for experimental use.
Research applications of recombinant VCL span *in vitro* assays (e.g., binding kinetics, structural analysis), cell biology (e.g., adhesion dynamics, force transduction), and disease models. Dysregulation of vinculin is implicated in pathologies like cancer metastasis, cardiovascular disorders, and wound-healing defects. By providing a controlled, scalable source of functional protein, recombinant VCL facilitates mechanistic insights into its biological roles and potential therapeutic targeting. Its utility extends to drug screening, biomechanical studies, and engineering synthetic matrices for regenerative medicine.
In summary, recombinant vinculin serves as a vital tool for dissecting the molecular basis of cell adhesion and mechanobiology, bridging structural biochemistry with translational applications.
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