| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FOPNL |
| Uniprot No | Q96NB1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-174aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MATVAELKAV LKDTLEKKGV LGHLKARIRA EVFNALDDDR EPRPSLSHEN LLINELIREY LEFNKYKYTA SVLIAESGQP VVPLDRQFLI HELNAFEESK DNTIPLLYGI LAHFLRGTKD GIQNAFLKGP SLQPSDPSLG RQPSRRKPMD DHLRKEEQKS TNIEDLHVSQ AVNR |
| 预测分子量 | 22 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. |
以下是模拟生成的关于FOPNL重组蛋白的参考文献示例(注：FOPNL为假设性命名，实际文献需通过学术数据库核实)：
1. **《高效表达FOPNL重组蛋白的大肠杆菌系统优化研究》**
- 作者：Zhang L, et al.
- 摘要：本研究通过密码子优化和诱导条件筛选，在大肠杆菌中实现了FOPNL重组蛋白的高效可溶性表达，并验证其体外结合活性，为规模化生产提供基础。
2. **《FOPNL重组蛋白在肿瘤细胞迁移抑制中的作用机制》**
- 作者：Wang Y, et al.
- 摘要：首次报道FOPNL重组蛋白通过调控Wnt/β-catenin通路抑制乳腺癌细胞侵袭，动物实验显示其显著降低肺转移灶形成。
3. **《基于杆状病毒系统的FOPNL重组蛋白糖基化修饰与功能分析》**
- 作者：Chen H, et al.
- 摘要：利用昆虫细胞表达体系获得正确糖基化修饰的FOPNL蛋白，证实其糖链结构对免疫细胞激活效力的关键影响。
4. **《FOPNL重组蛋白结构解析及其疫苗佐剂潜力评估》**
- 作者：Kimura T, et al.
- 摘要：通过冷冻电镜解析FOPNL三维结构，发现其特异性抗原表位;小鼠模型证明其作为新型疫苗佐剂可增强Th1型免疫应答。
建议通过PubMed、Web of Science等平台以“FOPNL recombinant protein”为关键词检索真实文献，或确认目标蛋白的标准命名。
**Background of FOPNL Recombinant Protein**
FOPNL (FGFR1OP N-terminal like) is a protein encoded by the *FOPNL* gene, which belongs to the FORMIN family. Initially identified through homology studies, FOPNL shares structural similarities with formin proteins, known for their roles in cytoskeleton regulation, particularly in actin polymerization and microtubule dynamics. FOPNL is implicated in cellular processes such as cell migration, vesicle trafficking, and cell division, though its precise molecular mechanisms remain under active investigation.
Recombinant FOPNL protein is artificially produced using biotechnological systems (e.g., *E. coli* or mammalian cell cultures) to enable functional and structural studies. By cloning the *FOPNL* gene into expression vectors, researchers can produce purified, high-quality protein for in vitro assays. This approach allows detailed analysis of FOPNL’s interactions with binding partners, its role in signaling pathways, and its potential involvement in diseases.
Studies suggest FOPNL may interact with components of the centrosome and cilia, linking it to ciliopathies or developmental disorders. Its dysregulation has also been observed in certain cancers, highlighting its potential as a therapeutic target. Recombinant FOPNL enables researchers to explore these associations, screen for inhibitors, and map domain-specific functions.
Current research focuses on resolving FOPNL’s 3D structure, post-translational modifications, and tissue-specific expression patterns. Its recombinant form serves as a critical tool for advancing our understanding of formin-related pathologies and developing targeted therapies.
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