| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VIL1 |
| Uniprot No | P09327 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-827aa |
| 氨基酸序列 | MTKLSAQVKGSLNITTPGLQIWRIEAMQMVPVPSSTFGSFFDGDCYIILAIHKTASSLSYDIHYWIGQDSSLDEQGAAAIYTTQMDDFLKGRAVQHREVQGNESEAFRGYFKQGLVIRKGGVASGMKHVETNSYDVQRLLHVKGKRNVVAGEVEMSWKSFNRGDVFLLDLGKLIIQWNGPESTRMERLRGMTLAKEIRDQERGGRTYVGVVDGENELASPKLMEVMNHVLGKRRELKAAVPDTVVEPALKAALKLYHVSDSEGNLVVREVATRPLTQDLLSHEDCYILDQGGLKIYVWKGKKANEQEKKGAMSHALNFIKAKQYPPSTQVEVQNDGAESAVFQQLFQKWTASNRTSGLGKTHTVGSVAKVEQVKFDATSMHVKPQVAAQQKMVDDGSGEVQVWRIENLELVPVDSKWLGHFYGGDCYLLLYTYLIGEKQHYLLYVWQGSQASQDEITASAYQAVILDQKYNGEPVQIRVPMGKEPPHLMSIFKGRMVVYQGGTSRTNNLETGPSTRLFQVQGTGANNTKAFEVPARANFLNSNDVFVLKTQSCCYLWCGKGCSGDEREMAKMVADTISRTEKQVVVEGQEPANFWMALGGKAPYANTKRLQEENLVITPRLFECSNKTGRFLATEIPDFNQDDLEEDDVFLLDVWDQVFFWIGKHANEEEKKAAATTAQEYLKTHPSGRDPETPIIVVKQGHEPPTFTGWFLAWDPFKWSNTKSYEDLKAELGNSRDWSQITAEVTSPKVDVFNANSNLSSGPLPIFPLEQLVNKPVEELPEGVDPSRKEEHLSIEDFTQAFGMTPAAFSALPRWKQQNLKKEKGLF |
| 预测分子量 | 92,6 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VIL1重组蛋白的3篇参考文献及其摘要概括：
1. **《Cloning and Expression of Recombinant Human Villin-1 in E. coli》**
*作者：Zhang, L. et al.*
摘要：本研究成功克隆了人源VIL1基因，并利用大肠杆菌表达系统实现了重组蛋白的高效表达。通过亲和层析纯化获得高纯度蛋白，经Western blot验证其抗原性，为后续功能研究奠定基础。
2. **《Functional Characterization of Recombinant VIL1 in Epithelial Cell Motility》**
*作者：Smith, J.R. & Patel, K.*
摘要：文章通过体外实验证明，重组VIL1蛋白可显著增强肠上皮细胞的迁移能力，并调控肌动蛋白纤维的重排。研究提示VIL1可能通过Rho-GTPase通路影响细胞运动。
3. **《Optimization of Recombinant VIL1 Production in Insect Cells for Structural Studies》**
*作者：Lee, S. et al.*
摘要：作者比较了昆虫细胞与哺乳动物系统表达重组VIL1的差异，发现昆虫系统产量更高且蛋白结晶性更优。通过冷冻电镜解析了VIL1的N端结构域三维构象。
(注：上述文献为示例性质，实际引用需以具体数据库检索结果为准。)
Vil1 (Villin-1) is a calcium-regulated actin-binding protein predominantly expressed in epithelial cells of the gastrointestinal tract, renal tubules, and sensory hair cells. It belongs to the gelsolin/villin superfamily, characterized by conserved gelsolin-like domains that enable actin filament severing, capping, and bundling. Vil1 plays a critical role in maintaining cell morphology, microvilli structure, and epithelial barrier function by modulating actin cytoskeleton dynamics. Its expression is tightly regulated during development and tissue-specific differentiation, making it a marker for absorptive enterocytes in the small intestine.
Recombinant Vil1 protein is engineered using expression systems (e.g., E. coli, mammalian cells) to produce purified, functional Vil1 for research and therapeutic applications. Studies leverage recombinant Vil1 to investigate its role in cell migration, polarization, and wound healing, as well as its involvement in pathological conditions such as inflammatory bowel disease (IBD) and cancer. In colorectal cancer, Vil1 overexpression is linked to tumor progression and metastasis, highlighting its potential as a diagnostic or prognostic biomarker.
The recombinant protein also serves as an antigen for antibody development, enabling targeted studies of Vil1's interactions with signaling molecules (e.g., Rho GTPases) or its calcium-dependent actin remodeling mechanisms. Additionally, it aids in structural analyses to resolve domain-specific functions, such as the N-terminal core’s actin-binding activity versus the C-terminal headpiece’s bundling properties. By providing a controlled, scalable source of Vil1. recombinant technology advances both basic research and translational efforts in epithelial biology and disease.
×
