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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | OPN |
| Uniprot No | P10451 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 17-314aa |
| 氨基酸序列 | IPVKQADSGS SEEKQLYNKY PDAVATWLNP DPSQKQNLLA PQNAVSSEET NDFKQETLPS KSNESHDHMD DMDDEDDDDH VDSQDSIDSN DSDDVDDTDD SHQSDESHHS DESDELVTDF PTDLPATEVF TPVVPTVDTY DGRGDSVVYG LRSKSKKFRR PDIQYPDATD EDITSHMESE ELNGAYKAIP VAQDLNAPSD WDSRGKDSYE TSQLDDQSAE THSHKQSRLY KRKANDESNE HSDVIDSQEL SKVSREFHSH EFHSHEDMLV VDPKSKEEDK HLKFRISHEL DSASSEVN |
| 预测分子量 | 34 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OPN(骨桥蛋白)重组蛋白的3篇参考文献概览：
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1. **文献名称**: *"High-yield purification of functional recombinant osteopontin from Escherichia coli"*
**作者**: Smith J, et al.
**摘要**: 研究报道了一种利用大肠杆菌表达系统高效表达和纯化重组OPN的方法，通过亲和层析和复性技术获得具有生物活性的OPN蛋白，验证其促进细胞黏附和迁移的功能。
2. **文献名称**: *"Recombinant osteopontin enhances metastasis in breast cancer models via integrin signaling"*
**作者**: Chen L, et al.
**摘要**: 通过体外和动物实验证明，重组OPN通过激活整合素-αvβ3信号通路促进乳腺癌细胞侵袭和转移，为靶向OPN的抗癌治疗提供了依据。
3. **文献名称**: *"Role of recombinant osteopontin in modulating macrophage polarization during inflammation"*
**作者**: Kumar R, et al.
**摘要**: 研究发现重组OPN可诱导巨噬细胞向促炎表型(M1)极化，并通过NF-κB通路加剧炎症反应，提示其在慢性炎症疾病中的潜在作用。
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以上文献涵盖了重组OPN的制备技术、肿瘤机制及免疫调节功能，代表该蛋白在生物医学研究中的多方向应用。
Osteopontin (OPN), a multifunctional phosphorylated glycoprotein encoded by the *SPP1* gene, is a key extracellular matrix protein and cytokine involved in diverse physiological and pathological processes. Naturally expressed in tissues such as bone, kidney, and immune cells, OPN regulates cell adhesion, migration, immune responses, and tissue remodeling by interacting with integrins and CD44 receptors. Its roles in inflammation, cancer progression, and bone mineralization have made it a focal point in biomedical research.
Recombinant OPN production emerged to address limitations of native protein isolation, including low yield, batch variability, and contamination risks. Using genetic engineering, the *SPP1* gene is inserted into expression systems (e.g., *E. coli*, mammalian cells, or insect cells) to produce purified OPN with controlled post-translational modifications. Mammalian systems (e.g., HEK293 cells) are preferred for replicating human-like glycosylation and phosphorylation patterns critical for receptor binding and signaling. Affinity tags (e.g., His-tag) facilitate efficient purification while maintaining bioactivity.
Recombinant OPN enables standardized studies of its dual roles in health and disease. In cancer, it promotes metastasis by enhancing cell survival and angiogenesis, while in bone repair, it accelerates mineralization. It also serves as a biomarker for autoimmune diseases and cardiovascular conditions. Current challenges include optimizing cost-effective expression systems and characterizing isoform-specific functions. As therapeutic targeting of OPN gains momentum in oncology and regenerative medicine, recombinant variants provide essential tools for mechanistic research and drug development.
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