| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | OPI |
| Uniprot No | P41145 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-380aa |
| 氨基酸序列 | MDSPIQIFRGEPGPTCAPSACLPPNSSAWFPGWAEPDSNGSAGSEDAQLEPAHISPAIPVIITAVYSVVFVVGLVGNSLVMFVIIRYTKMKTATNIYIFNLALADALVTTTMPFQSTVYLMNSWPFGDVLCKIVISIDYYNMFTSIFTLTMMSVDRYIAVCHPVKALDFRTPLKAKIINICIWLLSSSVGISAIVLGGTKVREDVDVIECSLQFPDDDYSWWDLFMKICVFIFAFVIPVLIIIVCYTLMILRLKSVRLLSGSREKDRNLRRITRLVLVVVAVFVVCWTPIHIFILVEALGSTSHSTAALSSYYFCIALGYTNSSLNPILYAFLDENFKRCFRDFCFPLKMRMERQSTSRVRNTVQDPAYLRDIDGMNKPV |
| 预测分子量 | 42,6 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OPI重组蛋白的3篇参考文献示例(注：以下内容为虚构，仅作示例参考)：
1. **《高效表达与纯化OPI重组蛋白及其抗炎活性研究》**
*作者：李明等*
摘要：本研究通过大肠杆菌表达系统成功克隆并表达了OPI重组蛋白，优化了诱导条件以提高可溶性表达。纯化后的蛋白在体外实验中显示出显著的抗炎效果，抑制了巨噬细胞中炎症因子的释放，为OPI的临床应用提供了实验依据。
2. **《OPI重组蛋白在骨质疏松模型中的治疗作用》**
*作者：Smith J, et al.*
摘要：通过哺乳动物细胞系(CHO)表达OPI重组蛋白，验证其抑制破骨细胞分化的功能。动物实验表明，该蛋白能显著改善骨质疏松模型小鼠的骨密度，机制可能与阻断RANKL信号通路相关。
3. **《基于酵母系统的OPI重组蛋白糖基化修饰及功能分析》**
*作者：张华等*
摘要：研究利用毕赤酵母系统表达糖基化修饰的OPI重组蛋白，发现糖基化显著增强了其稳定性和生物活性。通过体外细胞实验证实，修饰后的蛋白对肿瘤细胞迁移的抑制作用较未修饰版本提高约40%。
(注：实际文献需通过学术数据库检索确认，以上为模拟内容。)
**Background of OPI Recombinant Proteins**
Recombinant proteins, engineered through genetic modification, are pivotal in modern biotechnology and therapeutic development. OPI (Osteogenic Protein-1), a member of the TGF-β (transforming growth factor-beta) superfamily, is a notable example. Originally identified for its role in bone morphogenesis, OPI (also known as BMP-7. bone morphogenetic protein-7) regulates cellular processes such as differentiation, proliferation, and tissue repair, particularly in skeletal and renal systems. Its recombinant form, produced via heterologous expression systems (e.g., bacterial, mammalian, or insect cells), retains bioactivity while enabling scalable production for clinical and research applications.
The development of recombinant OPI emerged from the need to overcome limitations of natural protein extraction, such as low yield and contamination risks. By cloning the *OPI* gene into expression vectors, scientists achieve controlled synthesis with post-translational modifications tailored to mimic native functionality. Mammalian cell systems (e.g., CHO cells) are often preferred for complex folding requirements, whereas bacterial systems (e.g., *E. coli*) offer cost-effective production for structural studies.
Clinically, recombinant OPI has shown promise in treating orthopedic conditions, including non-union fractures and osteoarthritis, by stimulating osteoblast activity and cartilage regeneration. It also holds potential in regenerative medicine for kidney and neural tissue repair. However, challenges persist in optimizing stability, delivery mechanisms, and minimizing off-target effects. Advances in protein engineering, such as fusion tags or pegylation, aim to enhance pharmacokinetics and tissue specificity.
Research continues to explore OPI's broader therapeutic roles, leveraging its pleiotropic signaling pathways. As a recombinant therapeutic, OPI exemplifies the intersection of molecular biology and medicine, highlighting the importance of precision bioengineering in addressing unmet clinical needs.
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