| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | BSP |
| Uniprot No | P21815 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 129-281aa |
| 氨基酸序列 | AIQLPKKAGDITNKATKEKESDEEEEEEEEGNENEESEAEVDENEQGINGTSTNSTEAENGNGSSGGDNGEEGEEESVTGANAEDTTETGRQGKGTSKTTTSPNGGFEPTTPPQVYRTTSPPFGKTTTVEYEGEYEYTGANEYDNGYEIYESE |
| 预测分子量 | 32.4kDa |
| 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BSP(Bone Sialoprotein)重组蛋白的模拟参考文献示例，供参考使用。建议通过PubMed、Google Scholar等平台验证具体文献：
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1. **文献名称**: *Recombinant human bone sialoprotein promotes bone regeneration in a murine critical-size defect model*
**作者**: Valentin JE, et al.
**摘要**: 本研究利用大肠杆菌表达系统成功制备重组人BSP蛋白，并通过动物实验验证其促进骨缺损修复的能力。实验表明，局部应用重组BSP可显著增强成骨细胞分化及骨基质矿化，提示其在骨组织工程中的潜在应用。
2. **文献名称**: *Functional characterization of recombinant bovine seminal plasma proteins and their role in sperm motility*
**作者**: Plante G, et al.
**摘要**: 通过昆虫细胞表达系统生产重组牛BSP蛋白，分析其对精子功能的影响。结果显示，重组BSP能结合精子表面受体，提高精子活力和体外受精效率，为改善家畜繁殖技术提供了理论依据。
3. **文献名称**: *BSP-coated titanium implants enhance osteointegration via integrin-mediated signaling*
**作者**: Shibata Y, Matsumoto T.
**摘要**: 研究将重组BSP作为钛植入物涂层材料，发现其通过整合素信号通路促进成骨细胞黏附与增殖。体内实验显示，BSP涂层显著加速骨-植入物界面愈合，提示其在骨科植入物表面改性中的应用潜力。
4. **文献名称**: *Recombinant BSP facilitates breast cancer cell metastasis to bone through RANKL activation*
**作者**: Schneider JG, et al.
**摘要**: 利用哺乳动物细胞表达的重组BSP，揭示其通过激活RANKL通路促进乳腺癌细胞向骨组织迁移的机制。研究为靶向BSP抑制肿瘤骨转移提供了新思路。
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**注意**：以上文献信息为模拟示例，实际引用时请通过学术数据库核实作者、标题及摘要的准确性。若需具体领域文献，建议结合关键词(如“recombinant BSP protein bone”或“BSP recombinant reproduction”)进一步检索。
Bone sialoprotein (BSP), a phosphorylated glycoprotein predominantly found in mineralized tissues, plays a pivotal role in regulating hydroxyapatite crystal formation and osteoblast-mediated bone mineralization. As a key component of the extracellular matrix, BSP facilitates cell-matrix interactions through integrin-binding RGD motifs, contributing to bone remodeling and repair processes. Its expression is tightly regulated during osteogenic differentiation, making it a biomarker for bone formation. However, native BSP extraction from biological sources faces challenges including low abundance, structural complexity, and potential immunogenicity.
Recombinant BSP production emerged as a solution, leveraging genetic engineering to express and purify the protein in heterologous systems. Escherichia coli and mammalian expression systems are commonly employed, each offering distinct advantages: bacterial systems enable cost-effective production of non-glycosylated variants, while mammalian cells (e.g., CHO) preserve post-translational modifications crucial for biological activity. Advanced protein engineering techniques allow customization of BSP variants with enhanced stability, specific binding affinities, or reduced immunogenic potential.
Therapeutic applications of recombinant BSP span bone tissue engineering, dental regeneration, and osteointegration of implants. In regenerative medicine, it serves as a bioactive coating material to promote stem cell differentiation and accelerate bone defect healing. Pharmaceutical formulations incorporating recombinant BSP show promise in treating osteoporosis and fracture non-unions. Recent developments focus on creating fusion proteins combining BSP's mineralization domains with growth factors like BMP-2 to synergistically enhance osteogenic potential. Characterization challenges persist due to BSP's intrinsic disorder regions and calcium-dependent conformational changes, necessitating sophisticated analytical approaches for quality control. As biomaterial design evolves, recombinant BSP continues to offer versatile solutions for advanced orthopedic and dental therapies.
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