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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | OA |
| Uniprot No | Q08722 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-139aa |
| 氨基酸序列 | QLLFNKTKSVEFTFCNDTVVIPCFVTNMEAQNTTEVYVKWKFKGRDIYTF DGALNKSTVPTDFSSAKIEVSQLLKGDASLKMDKSDAVSHTGNYTCEVTE LTREGETIIELKYRVVSWFSP |
| 预测分子量 | 40 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3篇与骨关节炎(OA)相关重组蛋白研究的模拟参考文献示例(非真实文献，仅供格式参考)：
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1. **文献名称**: "High-yield expression and purification of recombinant human IL-1Ra in E. coli for osteoarthritis therapy"
**作者**: Smith, J. et al. (2020)
**摘要**: 研究通过大肠杆菌表达系统优化重组人IL-1受体拮抗剂(IL-1Ra)的产量，证明其可有效抑制OA模型中的炎症反应，为低成本生产抗OA药物提供方案。
2. **文献名称**: "Chondroprotective effects of recombinant TGF-β3 delivered via hydrogel in a rodent OA model"
**作者**: Zhang, L. et al. (2018)
**摘要**: 开发基于重组TGF-β3的水凝胶缓释系统，通过动物实验证实其能显著促进软骨修复并延缓OA进展，机制涉及激活软骨细胞合成代谢通路。
3. **文献名称**: "CRISPR-engineered CHO cells for producing glycosylated OA-targeting FGF18"
**作者**: Johnson, R. et al. (2019)
**摘要**: 利用基因编辑技术改造CHO细胞系，高效表达具有正确糖基化修饰的重组FGF18蛋白，体外实验显示其可增强软骨细胞增殖并减少基质降解。
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*注：以上文献为模拟内容，实际研究中建议通过PubMed或Web of Science检索真实文献(关键词：recombinant protein, osteoarthritis, IL-1Ra, FGF18等)。*
**Background of OA Recombinant Protein**
Recombinant proteins are engineered through genetic modification, enabling the production of specific proteins in host systems like *E. coli*, yeast, or mammalian cells. This technology offers precise control over protein structure, ensuring high purity and reproducibility compared to traditional extraction methods. OA (Ovalbumin) recombinant protein, derived from the chicken egg white protein ovalbumin, is a well-characterized model antigen widely used in immunological and biomedical research.
OA is a 45 kDa glycoprotein belonging to the serpin family, though it lacks protease inhibitory activity. Its recombinant form is produced by inserting the ovalbumin gene into expression vectors, followed by purification via chromatography. This method eliminates batch variability and contaminants associated with native extraction, making it ideal for standardized experiments.
In research, OA recombinant protein is pivotal in studying immune responses, particularly in allergy and asthma models. It serves as an antigen to induce hypersensitivity in animal studies, aiding mechanistic investigations of Th2-mediated inflammation. Additionally, it is employed in vaccine development, antigen-antibody interaction studies, and as a reference in diagnostic assays. Its compatibility with *in vitro* and *in vivo* systems underscores its versatility.
Beyond basic research, OA recombinant protein is utilized in drug screening, particularly for validating therapeutic antibodies or immunomodulators. Its scalability and cost-effectiveness in microbial hosts (e.g., *E. coli*) further enhance its accessibility. As personalized medicine advances, OA recombinant protein remains a critical tool for understanding immune pathologies and accelerating therapeutic innovation.
This blend of reliability, adaptability, and relevance ensures OA recombinant protein’s enduring role in bridging molecular biology with clinical applications.
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