| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | bop |
| Uniprot No | P33972 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 149-166aa |
| 氨基酸序列 | SLSGRVANLPSDTRSTFK |
| 预测分子量 | 18.0 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BOP重组蛋白的参考文献示例(内容为虚构，仅作格式参考)：
1. **《Structural Analysis of BOP Complex in Bacterial Outer Membrane Biogenesis》**
*作者：Zhang Y, et al.*
*摘要：* 通过冷冻电镜解析了BOP复合物的三维结构，揭示了其在细菌外膜蛋白折叠与组装中的分子机制，为优化重组膜蛋白表达提供理论依据。
2. **《Engineering BOP Chaperones to Enhance Recombinant Protein Solubility in E. coli》**
*作者：Kim S, Patel R*
*摘要：* 通过改造BOP复合物的分子伴侣组分，显著提升了大肠杆菌中难溶性重组蛋白的溶解度和稳定性，应用于工业级蛋白生产。
3. **《BOP-Mediated Folding Pathways of β-Barrel Proteins in Synthetic Membranes》**
*作者：Müller T, et al.*
*摘要：* 在人工膜体系中重构BOP复合物功能，阐明其介导β-桶状蛋白的折叠路径，为体外重组膜蛋白制备提供新方法。
4. **《Functional Crosstalk between BOP and Secretion Systems in Recombinant Protein Secretion》**
*作者：Itoh N, et al.*
*摘要：* 研究BOP复合物与细菌分泌系统的协同作用，优化重组蛋白跨膜转运效率，为高效分泌表达系统的设计奠定基础。
(注：以上文献为模拟示例，实际研究中请查阅真实数据库获取权威信息。)
**Background of BOP Recombinant Proteins**
BOP (Bivalent Oligopeptide Platform) recombinant proteins represent a class of engineered proteins designed to enhance specificity and functionality in biomedical applications. These proteins are constructed by fusing functional domains—such as binding motifs, enzymatic regions, or signaling sequences—with flexible peptide linkers, enabling dual-target engagement or multifunctional activity. The BOP framework leverages recombinant DNA technology, where genes encoding specific protein domains are cloned, modified, and expressed in host systems (e.g., *E. coli*, yeast, or mammalian cells), followed by purification to achieve high yields of functional proteins.
The design of BOP proteins often focuses on addressing challenges in therapeutic targeting, such as low affinity, poor stability, or off-target effects. For instance, bivalent or multivalent structures in BOP proteins can improve binding avidity to cell surface receptors (e.g., growth factor receptors or immune checkpoints) compared to monovalent counterparts. This property is particularly valuable in oncology, where dual-targeting BOP proteins may inhibit multiple signaling pathways in cancer cells or simultaneously engage immune cells and tumor antigens for enhanced immunotherapy.
Beyond therapeutics, BOP recombinant proteins are utilized in diagnostics, biosensing, and basic research. Their modular architecture allows customization for detecting biomarkers, delivering payloads (e.g., drugs, imaging agents), or studying protein-protein interactions. Advances in computational modeling and structural biology have further refined BOP designs, enabling precise control over spatial arrangement and functional synergy between domains.
Despite their promise, challenges remain, including optimizing expression systems for complex multidomain proteins, minimizing immunogenicity, and ensuring scalability for clinical use. Ongoing research aims to expand the versatility of BOP platforms, integrating novel domains (e.g., CRISPR components or synthetic peptides) to unlock next-generation biotherapeutics and tools for precision medicine.
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