| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SMTN |
| Uniprot No | P53814 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-917aa |
| 氨基酸序列 | MADEALAGLDEGALRKLLEVTADLAERRRIRSAIRELQRQELEREEEALASKRFRAERQDNKENWLHSQQREAEQRAALARLAGQLESMNDVEELTALLRSAGEYEERKLIRAAIRRVRAQEIEAATLAGRLYSGRPNSGSREDSKGLAAHRLEQCEVPEREEQEQQAEVSKPTPTPEGTSQDVTTVTLLLRAPPGSTSSSPASPSSSPTPASPEPPLEPAEAQCLTAEVPGSPEPPPSPPKTTSPEPQESPTLPSTEGQVVNKLLSGPKETPAAQSPTRGPSDTKRADVAGPRPCQRSLSVLSPRQPAQNRESTPLASGPSSFQRAGSVRDRVHKFTSDSPMAARLQDGTPQAALSPLTPARLLGPSLTSTTPASSSSGSSSRGPSDTSSRFSKEQRGVAQPLAQLRSCPQEEGPRGRGLAARPLENRAGGPVARSEEPGAPLPVAVGTAEPGGSMKTTFTIEIKDGRGQASTGRVLLPTGNQRAELTLGLRAPPTLLSTSSGGKSTITRVNSPGTLARLGSVTHVTSFSHAPPSSRGGCSIKMEAEPAEPLAAAVEAANGAEQTRVNKAPEGRSPLSAEELMTIEDEGVLDKMLDQSTDFEERKLIRAALRELRQRKRDQRDKERERRLQEARGRPGEGRGNTATETTTRHSQRAADGSAVSTVTKTERLVHSNDGTRTARTTTVESSFVRRSENGSGSTMMQTKTFSSSSSSKKMGSIFDREDQASPRAGSLAALEKRQAEKKKELMKAQSLPKTSASQARKAMIEKLEKEGAAGSPGGPRAAVQRSTSFGVPNANSIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPEAFDYGQLSPQNRRQNFEVAFSSAEMLVDCVPLVEVDDMMIMGKKPDPKCVFTYVQSLYNHLRRHELRLRGKNV |
| 预测分子量 | 99 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SMTN(Supervillin)重组蛋白研究的3篇虚构参考文献示例，涵盖不同研究方向和内容：
1. **文献名称**：*Recombinant SMTN Expression in E. coli and Its Role in Actin Cytoskeleton Regulation*
**作者**：Zhang L., et al.
**摘要**：本研究成功构建了SMTN重组蛋白的原核表达系统，优化纯化条件后获得高纯度蛋白。体外实验表明，重组SMTN通过与F-actin结合调控细胞骨架动态组装，为研究其细胞迁移功能提供了工具。
2. **文献名称**：*Structural Characterization of Human SMTN Isoform IV by Cryo-EM*
**作者**：Wang Y., et al.
**摘要**：利用冷冻电镜解析了SMTN异构体IV的重组蛋白三维结构，揭示了其N端膜结合域与C端actin结合域的构象特征，为理解SMTN在细胞膜-骨架信号转导中的作用机制提供了结构基础。
3. **文献名称**：*SMTN Recombinant Protein Enhances Metastatic Potential of Breast Cancer Cells In Vivo*
**作者**：Chen H., et al.
**摘要**：通过重组SMTN蛋白处理实验，发现其能显著促进乳腺癌细胞侵袭和转移，机制涉及整合素信号通路的激活。该研究提示SMTN可能成为癌症治疗的潜在靶点。
注：以上文献信息为示例性虚构内容，实际研究中建议通过PubMed/Google Scholar检索真实文献(关键词：Supervillin recombinant protein)。
**Background of SMTN Recombinant Protein**
SMTN (schwannomin-merlin-talin-N-terminal-like) recombinant protein is a engineered biomolecule derived from the SMTN gene, which encodes a cytoskeletal protein involved in cellular structure organization, signaling, and mechanical stability. The native SMTN protein shares functional domains with merlin (moesin-ezrin-radixin-like protein), a tumor suppressor linked to neurofibromatosis type 2 (NF2), and talin, a key mediator of integrin-mediated cell adhesion. These domains enable SMTN to interact with membrane-associated proteins, actin filaments, and signaling complexes, playing roles in cell motility, proliferation, and apoptosis regulation.
Recombinant SMTN is produced via heterologous expression systems, such as *E. coli* or mammalian cell cultures, to ensure high purity and bioactivity for research applications. Its production enables detailed studies of SMTN’s molecular interactions, particularly in cancer biology and neurodegenerative diseases, where cytoskeletal dysregulation is implicated. For instance, SMTN’s homology to merlin suggests potential involvement in tumor suppression pathways, while its talin-like domains may contribute to understanding metastasis or cell-matrix adhesion defects.
In drug discovery, recombinant SMTN serves as a tool for screening therapeutic compounds targeting cytoskeletal abnormalities or restoring tumor suppressor functions. It is also utilized in structural studies to map binding sites for partner proteins or to engineer mutants for functional assays. Despite its utility, challenges remain in mimicking post-translational modifications critical for native SMTN activity, necessitating optimized expression systems. Ongoing research aims to clarify SMTN’s physiological roles and its potential as a diagnostic marker or therapeutic target in diseases marked by cytoskeletal instability.
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