| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FN |
| Uniprot No | P02751 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 全长 |
| 氨基酸序列 | full |
| 预测分子量 | 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篇关于FN(纤维连接蛋白)重组蛋白的参考文献示例，涵盖生产方法及应用领域：
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1. **文献名称**: "High-yield production of recombinant fibronectin in *E. coli* and its application in cell culture"
**作者**: Zhang, Y., Wang, L., & Chen, X.
**摘要**: 本研究开发了一种通过大肠杆菌高效表达重组FN的方法，优化了表达条件与纯化工艺，证明重组FN在支持细胞粘附、铺展及增殖方面的性能与天然FN相当，可替代高价天然蛋白用于体外细胞培养。
2. **文献名称**: "Engineered fibronectin fragments as modular components for tailored cell adhesion"
**作者**: Brown, A.L., & Heilshorn, S.C.
**摘要**: 通过基因工程将FN的RGD(精氨酸-甘氨酸-天冬氨酸)和PHSRN(协同结合域)序列重组，设计出模块化FN片段。实验表明这些片段可精确调控细胞粘附强度与特异性，为组织工程支架提供定制化解决方案。
3. **文献名称**: "Recombinant fibronectin matrix enhances mesenchymal stem cell proliferation and differentiation"
**作者**: Kim, H., Park, J., & Lee, K.
**摘要**: 利用重组FN包被培养表面，显著提升了间充质干细胞的增殖速率及成骨分化效率，证实其在骨组织再生中的潜在应用价值，为干细胞治疗提供优化培养体系。
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**备注**：以上文献信息为示例性质，实际引用时建议通过学术数据库(如PubMed、Web of Science)核实具体文献的标题、作者及摘要内容，确保准确性。
Fibronectin (FN) is a high-molecular-weight glycoprotein found in extracellular matrices (ECMs) and plasma, playing critical roles in cell adhesion, migration, differentiation, and tissue repair. It consists of modular domains, including type III repeats that mediate interactions with integrins, collagen, and other ECM components. Recombinant FN proteins are engineered versions produced via genetic engineering techniques, typically using bacterial (e.g., *E. coli*) or mammalian expression systems. These proteins retain key functional domains, such as the RGD (Arg-Gly-Asp) motif in the III-10 domain, which binds integrins to regulate cell signaling.
The development of recombinant FN emerged to overcome limitations of plasma-derived FN, such as batch variability, pathogen risks, and difficulty in modifying specific domains. By leveraging recombinant DNA technology, researchers can tailor FN fragments with enhanced stability, altered binding affinities, or fused functional tags for targeted applications. For example, engineered FN fragments are used to functionalize biomaterials, promote cell attachment in *in vitro* cultures, or mimic ECM microenvironments in tissue engineering. They also serve as tools to study cancer metastasis, as tumor cells often dysregulate FN-integrin interactions during invasion.
Recent advances focus on creating FN-based hybrids or chimeric proteins for drug delivery, wound healing, and regenerative medicine. For instance, FN fragments conjugated with growth factors or antimicrobial peptides show promise in accelerating tissue repair. Additionally, recombinant FN variants with tunable mechanical properties are explored for 3D bioprinting and organoid development. Overall, recombinant FN proteins bridge fundamental ECM biology with translational innovations, offering scalable, customizable solutions for biomedical research and therapeutic development.
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