| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ON |
| Uniprot No | P13725 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-221aa |
| 氨基酸序列 | AAIGSCSKEY RVLLGQLQKQ TDLMQDTSRL LDPYIRIQGL DVPKLREHCR ERPGAFPSEE TLRGLGRRGF LQTLNATLGC VLHRLADLEQ RLPKAQDLER SGLNIEDLEK LQMARPNILG LRNNIYCMAQ LLDNSDTAEP TKAGRGASQP PTPTPASDAF QRKLEGCRFL HGYHRFMHSV GRVFSKWGES PNRSRR |
| 预测分子量 | 22 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(假设“ON重组蛋白”指某类特定重组蛋白研究)的模拟参考文献示例，供参考(实际文献请通过学术数据库查询)：
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1. **文献名称**：Optimized Expression and Purification of ON Recombinant Protein in E. coli
**作者**：Zhang, L. et al.
**摘要**：本研究建立了一种高效表达ON重组蛋白的大肠杆菌系统，通过密码子优化和诱导条件调控，将蛋白产量提升至120 mg/L，并利用亲和层析技术获得高纯度产物，为后续功能研究奠定基础。
2. **文献名称**：Structural Analysis of ON Recombinant Protein and Its Role in Cell Signaling
**作者**：Kim, S., & Patel, R.
**摘要**：通过X射线晶体学解析ON重组蛋白的三维结构，发现其N端结构域与配体结合的关键位点，并证实该蛋白通过激活MAPK通路调控细胞增殖，为靶向药物设计提供依据。
3. **文献名称**：Functional Characterization of ON Recombinant Protein in Neurodegenerative Models
**作者**：Gupta, A. et al.
**摘要**：在阿尔茨海默病模型中，ON重组蛋白表现出抑制β-淀粉样蛋白聚集的能力，并减少神经元凋亡，提示其潜在治疗神经退行性疾病的应用价值。
4. **文献名称**：Large-Scale Production of ON Recombinant Protein Using Mammalian Cell Culture
**作者**：Müller, J., & Schmidt, F.
**摘要**：开发基于CHO细胞的稳定表达体系，实现ON重组蛋白的规模化生产(纯度>98%)，并通过动物实验验证其与天然蛋白等效的生物活性，满足临床前试验需求。
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**注意**：以上内容为模拟示例，具体文献需通过PubMed、Google Scholar等平台检索关键词(如“recombinant protein expression”、“ON protein function”)。若“ON”指特定蛋白(如Osteonectin等)，请补充说明以精确检索。
**Background of Recombinant ON Protein**
Recombinant ON (osteonectin) protein, also known as SPARC (Secreted Protein Acidic and Rich in Cysteine), is a multifunctional glycoprotein involved in extracellular matrix (ECM) remodeling, cell-matrix interactions, and tissue repair. Initially identified in bone, ON is widely expressed in tissues undergoing active morphogenesis or repair, such as during embryogenesis, wound healing, and pathological conditions like fibrosis and cancer. Its structure includes distinct domains that mediate interactions with collagen, growth factors (e.g., VEGF, PDGF), and cell surface receptors, enabling roles in angiogenesis, cell adhesion, and modulation of growth factor signaling.
The recombinant form of ON is produced via genetic engineering, typically using bacterial (e.g., *E. coli*), yeast, or mammalian expression systems. This allows large-scale, high-purity production for research and therapeutic applications. Recombinant ON retains bioactivity, facilitating studies on its dual role in both promoting and inhibiting tumor progression—context-dependent effects linked to its ability to regulate ECM stiffness, immune responses, and metastatic pathways.
In biomedical research, recombinant ON is utilized to explore tissue regeneration mechanisms, cancer biology, and fibrotic diseases. It also holds potential in regenerative medicine, such as designing biomaterials to enhance bone or cartilage repair. Challenges include understanding its paradoxical roles in different microenvironments and optimizing delivery strategies for clinical use. Overall, recombinant ON remains a critical tool for deciphering ECM dynamics and developing targeted therapies.
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