| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | OGN |
| Uniprot No | P20774 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-298aa |
| 氨基酸序列 | PPTQQDSRIIYDYGTDNFEESIFSQDYEDKYLDGKNIKEKETVIIPNEKSLQLQKDEAITPLPPKKENDEMPTCLLCVCLSGSVYCEEVDIDAVPPLPKESAYLYARFNKIKKLTAKDFADIPNLRRLDFTGNLIEDIEDGTFSKLSLLEELSLAENQLLKLPVLPPKLTLFNAKYNKIKSRGIKANAFKKLNNLTFLYLDHNALESVPLNLPESLRVIHLQFNNIASITDDTFCKANDTSYIRDRIEEIRLEGNPIVLGKHPNSFICLKRLPIGSYF |
| 预测分子量 | 33.7kDa |
| 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OGN(骨糖蛋白，Osteoglycin)重组蛋白功能的3篇示例文献参考(注：以下内容为基于领域知识的假设性示例，建议通过学术数据库核实具体文献)：
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1. **文献名称**: *"Recombinant Osteoglycin Enhances Cartilage Repair in a Rat Osteoarthritis Model"*
**作者**: Smith J, et al.
**摘要**: 研究证明，重组OGN蛋白可通过激活Smad信号通路促进软骨细胞外基质合成，显著改善大鼠骨关节炎模型的软骨损伤，表明其在软骨再生中的治疗潜力。
2. **文献名称**: *"Osteoglycin Recombinant Protein Attenuates Cardiac Fibrosis via Modulating TGF-β1 Signaling"*
**作者**: Chen L, et al.
**摘要**: 该文献发现重组OGN蛋白能够抑制成纤维细胞向肌成纤维细胞转化，通过下调TGF-β1/Smad3通路减轻小鼠心脏纤维化，提示其在抗纤维化治疗中的应用价值。
3. **文献名称**: *"Recombinant Osteoglycin Suppresses Breast Cancer Metastasis by Inhibiting Integrin-β1/FAK Pathway"*
**作者**: Wang Y, et al.
**摘要**: 实验表明，重组OGN通过阻断整合素-β1与细胞外基质的相互作用，抑制FAK磷酸化，从而降低乳腺癌细胞的迁移和侵袭能力，揭示其作为肿瘤转移抑制因子的机制。
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**建议**：可通过PubMed、Web of Science等平台，以关键词“recombinant Osteoglycin”、“OGN protein function”检索最新研究，重点关注其在组织修复、疾病机制或生物材料中的应用。
**Background of OGN Recombinant Protein**
Osteoglycin (OGN), also known as mimecan, is a small leucine-rich proteoglycan (SLRP) initially identified for its role in bone and extracellular matrix (ECM) organization. It regulates collagen fibrillogenesis, cell adhesion, and tissue repair. OGN is expressed in various tissues, including skeletal, cardiovascular, and ocular systems, and has been implicated in modulating signaling pathways related to cell proliferation, differentiation, and inflammation.
Recombinant OGN protein is produced using biotechnological platforms, such as *E. coli* or mammalian cell systems, enabling large-scale, high-purity yields for research and therapeutic applications. Its recombinant form retains biological activity, allowing studies on its molecular interactions and mechanisms.
OGN's dual role in homeostasis and disease has driven interest. In pathologies, OGN dysregulation is linked to cancer progression, fibrosis, and cardiovascular diseases. For instance, it acts as a tumor suppressor in some cancers but promotes metastasis in others, highlighting context-dependent functions. Recombinant OGN aids in deciphering these complexities, serving as a tool for *in vitro* and *in vivo* disease modeling, drug screening, and biomarker discovery.
Current research focuses on OGN’s therapeutic potential—exploring its use in tissue engineering, wound healing, or as a target for biologics. However, challenges remain, including understanding isoform-specific effects and optimizing delivery systems. Advances in recombinant protein engineering and personalized medicine may unlock OGN’s full translational value, bridging ECM biology with clinical innovation.
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