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| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Osteopontin |
| 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Osteopontin(OPN)重组蛋白的模拟参考文献示例(实际文献需通过学术数据库查询)：
1. **标题**: "Recombinant Osteopontin Promotes Bone Regeneration in a Mouse Model of Critical-Sized Defects"
**作者**: Smith A, et al.
**摘要**: 研究利用大肠杆菌表达的重组OPN蛋白，通过动物模型证明其能显著增强骨缺损区域的成骨细胞分化和矿化，促进骨组织再生。
2. **标题**: "Osteopontin Modulates Immune Responses in Sepsis via Recombinant Protein Delivery"
**作者**: Chen L, et al.
**摘要**: 通过哺乳动物细胞系统表达的重组OPN，发现其通过调控巨噬细胞极化减轻脓毒症模型中的炎症反应，揭示其免疫调节功能。
3. **标题**: "Expression and Purification of Functional Recombinant Osteopontin in Pichia pastoris"
**作者**: Kim J, et al.
**摘要**: 优化了毕赤酵母系统中OPN重组蛋白的表达和纯化工艺，验证其磷酸化修饰对肿瘤细胞迁移的促进作用，为癌症研究提供工具。
4. **标题**: "Osteopontin-Coated Biomaterials Enhance Osseointegration in Dental Implants"
**作者**: Zhang Y, et al.
**摘要**: 将重组OPN作为钛合金种植体表面涂层，证明其可显著提升体内骨结合效率，降低植入失败率。
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**注意**：以上为示例性内容，具体文献需通过PubMed、Google Scholar等平台检索关键词(如"recombinant osteopontin" + 研究领域)。实际引用时需核对作者、期刊及年份准确性。
Osteopontin (OPN), also known as secreted phosphoprotein 1 (SPP1), is a multifunctional extracellular matrix glycoprotein involved in diverse physiological and pathological processes. It belongs to the SIBLING (Small Integrin-Binding Ligand N-linked Glycoprotein) family and is characterized by conserved structural motifs, including an Arg-Gly-Asp (RGD) integrin-binding domain and binding sites for CD44 receptors. OPN plays critical roles in cell adhesion, migration, immune regulation, tissue remodeling, and biomineralization, with implications in cancer progression, inflammatory diseases, bone metabolism, and cardiovascular disorders.
Recombinant osteopontin is produced using genetic engineering techniques, typically expressed in prokaryotic (e.g., E. coli) or eukaryotic systems (e.g., mammalian cells, insect cells). The choice of expression system depends on the need for post-translational modifications, such as phosphorylation and glycosylation, which significantly influence OPN's bioactivity. Bacterial systems offer cost-effective production but lack native modifications, while mammalian systems yield proteins closer to human OPN's natural structure. Researchers often purify recombinant OPN via affinity tags to study its isoform-specific functions or therapeutic potential.
Its applications span basic research—elucidating mechanisms in metastasis, osteoclastogenesis, or immune responses—and translational studies, including biomarker discovery or regenerative medicine. Challenges persist in replicating OPN's complex modification patterns and resolving functional differences between full-length and cleaved isoforms. Ongoing work aims to optimize recombinant OPN production for consistency in preclinical models and potential clinical use, particularly in tissue engineering and targeted therapies.
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