| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SMURF1 |
| Uniprot No | Q9HCE7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 198-374aa |
| 氨基酸序列 | VESPSQDQRLQAQRLRNPDVRGSLQTPQNRPHGHQSPELPEGYEQRTTVQGQVYFLHTQTGVSTWHDPRIPSPSGTIPGGDAAFLYEFLLQGHTSEPRDLNSVNCDELGPLPPGWEVRSTVSGRIYFVDHNNRTTQFTDPRLHHIMNHQCQLKEPSQPLPLPSEGSLEDEELPAQRY |
| 预测分子量 | 24.1 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SMURF1重组蛋白的3篇代表性文献示例(注：文献信息为示例，非真实存在)：
1. **"Recombinant SMURF1 mediates ubiquitination of SMAD proteins in vitro"**
- **作者**: Zhang Q, Wang L, et al.
- **摘要**: 该研究通过大肠杆菌表达系统成功纯化重组SMURF1蛋白，验证其体外泛素化SMAD1和SMAD5的能力，揭示SMURF1在TGF-β/BMP信号通路中的负调控机制。
2. **"Structural insights into the HECT domain of SMURF1 and its ubiquitin ligase activity"**
- **作者**: Wiesner S, et al.
- **摘要**: 利用X射线晶体学解析重组SMURF1的HECT结构域三维结构，阐明其与泛素结合的关键位点及催化泛素转移的分子机制。
3. **"SMURF1 recombinant protein inhibits cancer metastasis by targeting RhoA degradation"**
- **作者**: Li H, Chen X, et al.
- **摘要**: 通过哺乳动物细胞表达系统获得功能性重组SMURF1.证明其通过泛素化降解RhoA蛋白抑制肿瘤细胞迁移和侵袭，为癌症治疗提供潜在靶点。
4. **"Functional characterization of a truncated SMURF1 variant in bone formation"**
- **作者**: Chen M, et al.
- **摘要**: 研究构建并纯化截短型SMURF1重组蛋白，发现其通过调节Runx2的稳定性促进成骨细胞分化，为骨代谢疾病研究提供新方向。
(注：以上文献为模拟示例，实际研究中请通过PubMed或Google Scholar检索真实文献。)
SMURF1 (SMAD-specific E3 ubiquitin-protein ligase 1) is a member of the HECT family of E3 ubiquitin ligases, playing a critical role in regulating cellular processes via the ubiquitin-proteasome system. It mediates the targeted degradation of substrate proteins by attaching ubiquitin molecules, marking them for proteasomal destruction. Structurally, SMURF1 contains two N-terminal WW domains for substrate recognition and a C-terminal HECT domain responsible for ubiquitin transfer. Its activity is tightly regulated through post-translational modifications and interactions with signaling molecules.
Functionally, SMURF1 is best known for its role in modulating TGF-β/BMP signaling pathways. It ubiquitinates key mediators like SMADs and receptors, influencing cell differentiation, apoptosis, and tissue homeostasis. Beyond TGF-β/BMP regulation, SMURF1 interacts with non-SMAD targets, including RhoA and MEKK2. impacting cell polarity, migration, and MAPK signaling. Its involvement in diverse pathways underscores its importance in embryonic development, tissue repair, and disease pathogenesis.
In disease contexts, SMURF1 exhibits dual roles. It acts as a tumor suppressor by degrading oncogenic substrates but can promote cancer metastasis through cytoskeletal remodeling. It also contributes to fibrosis by enhancing fibroblast activation and matrix deposition. These paradoxical effects highlight its context-dependent functionality.
Recombinant SMURF1 protein, typically produced in bacterial or mammalian systems, retains enzymatic activity and is widely used to study ubiquitination mechanisms, screen modulators, and explore therapeutic interventions. Tagged versions (e.g., His, GST) facilitate purification and detection. Current research focuses on targeting SMURF1 for treating cancers, fibrotic disorders, and bone diseases, leveraging its regulatory role in critical cellular pathways. Its dual functionality poses challenges but also opens avenues for precision therapeutic strategies.
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