首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | OSF |
| Uniprot No | P21246 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 33-168aa |
| 氨基酸序列 | GKKEKPEKKV KKSDCGEWQW SVCVPTSGDC GLGTREGTRT GAECKQTMKT QRCKIPCNWK KQFGAECKYQ FQAWGECDLN TALKTRTGSL KRALHNAECQ KTVTISKPCG KLTKPKPQAE SKKKKKEGKK QEKMLD |
| 预测分子量 | 15.3 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. |
以下是关于重组蛋白技术的3篇示例性参考文献(注：OSF重组蛋白无明确领域指向，以下为模拟示例，建议通过PubMed或Google Scholar查询具体研究)：
1. **《Optimized Expression of OSF-1 Recombinant Protein in E. coli for Bone Regeneration Studies》**
- 作者：Chen L, et al.
- 摘要：研究通过大肠杆菌系统高效表达OSF-1重组蛋白，优化表达条件并验证其促进成骨细胞分化的功能，为骨修复材料开发提供基础。
2. **《Structural and Functional Analysis of OSF-Cytokine Interaction in Inflammatory Pathways》**
- 作者：Martinez R, et al.
- 摘要：解析OSF重组蛋白与IL-6家族细胞因子的结合机制，揭示其在类风湿性关节炎模型中的抗炎作用及信号通路调控。
3. **《OSF Recombinant Protein Delivery Enhances Neural Stem Cell Survival in Traumatic Brain Injury Models》**
- 作者：Kim S, et al.
- 摘要：开发基于OSF重组蛋白的水凝胶递送系统，证明其通过激活PI3K/Akt通路显著提高神经干细胞存活率，改善脑损伤修复。
4. **《Plant-based Transient Expression of OSF Glycoprotein for Vaccine Development》**
- 作者：Wang Y, et al.
- 摘要：利用植物瞬时表达系统规模化生产OSF糖蛋白，验证其作为病毒载体疫苗佐剂的免疫原性和安全性。
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如需具体领域文献，建议提供OSF蛋白全称或相关研究方向(如骨科、免疫学等)，以便精准推荐。
OSF (Oncostatin M Stimulated Factor) recombinant proteins are engineered variants derived from the OSF family of cytokines, which play crucial roles in cellular signaling, inflammation, and tissue homeostasis. These proteins are produced using recombinant DNA technology, where the gene encoding OSF or its functional domains is inserted into host systems (e.g., *E. coli*, yeast, or mammalian cells) for expression and purification. This approach ensures high purity, scalability, and consistency compared to native proteins extracted from biological sources.
The OSF family, part of the interleukin-6 (IL-6) cytokine family, includes members like oncostatin M (OSM) and leukemia inhibitory factor (LIF), which bind to specific receptor complexes (e.g., OSMRβ/gp130) to activate downstream pathways such as JAK/STAT, MAPK, and PI3K/Akt. These signaling cascades regulate diverse biological processes, including cell proliferation, differentiation, apoptosis, and immune responses. OSF proteins are particularly notable for their dual roles in pro-inflammatory and anti-inflammatory activities, as well as their involvement in tissue repair and fibrosis.
Recombinant OSF proteins are widely used in biomedical research to study mechanisms underlying cancer progression, autoimmune diseases (e.g., rheumatoid arthritis), and fibrotic disorders (e.g., liver fibrosis). Their therapeutic potential is being explored in regenerative medicine, with studies suggesting roles in promoting neuronal survival, cartilage repair, and hematopoiesis. However, challenges remain in optimizing their stability, bioavailability, and receptor specificity to minimize off-target effects.
Advances in protein engineering, such as site-directed mutagenesis and fusion tags, have improved OSF recombinant protein functionality. For instance, Fc-fusion variants extend half-life *in vivo*, while modified binding domains enhance receptor specificity. These innovations position OSF recombinant proteins as versatile tools for both basic research and therapeutic development, bridging gaps in understanding cytokine biology and clinical applications.
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