| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FN1 |
| Uniprot No | P02751 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 732-911aa |
| 氨基酸序列 | TASSFVVSWVSASDTVSGFRVEYELSEEGDEPQYLDLPSTATSVNIPDLLPGRKYIVNVYQISEDGEQSLILSTSQTTAPDAPPDPTVDQVDDTSIVVRWSRPQAPITGYRIVYSPSVEGSSTELNLPETANSVTLSDLQPGVQYNITIYAVEENQESTPVVIQQETTGTPRSDTVPSPR |
| 预测分子量 | 23.6 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FN1重组蛋白的3篇文献示例(注：以下内容为模拟文献，实际引用时请核实原文信息)：
1. **文献名称**：Recombinant human fibronectin extra domain B enhances osteoblast adhesion and differentiation
**作者**：Zhang Y, et al.
**摘要**：研究通过重组技术表达FN1的特定结构域(EDB)，证明其能显著促进成骨细胞黏附和分化，为骨组织工程提供潜在应用。
2. **文献名称**：High-yield production of FN1 fragment in E. coli and its functional characterization in wound healing
**作者**：Li H, Wang X.
**摘要**：报道了一种大肠杆菌表达系统高效生产FN1重组蛋白片段的方法，并通过体外实验验证其加速伤口愈合的生物学活性。
3. **文献名称**：Structural analysis of recombinant FN1 type III domains using cryo-EM
**作者**：Chen R, et al.
**摘要**：利用冷冻电镜解析了重组表达的FN1 III型结构域三维构象，揭示了其与整合素结合的分子机制，为靶向药物设计提供结构基础。
提示：实际研究中建议通过PubMed或Web of Science搜索关键词 "recombinant FN1 protein" + "expression/application/structure"，筛选近5年高被引论文获取最新进展。
Fibronectin-1 (FN1) recombinant protein is a engineered version of the extracellular matrix glycoprotein fibronectin, a critical mediator of cell adhesion, migration, and signaling. Naturally produced as a high-molecular-weight (~440 kDa) dimer by hepatocytes and various cell types, fibronectin exists in two primary forms: soluble plasma fibronectin and insoluble cellular fibronectin. The recombinant FN1 protein is typically generated using expression systems (e.g., mammalian, bacterial, or insect cells) to produce specific domains or full-length variants, often excluding the alternative splicing domains (e.g., EDA or EDB) present in tissue-specific isoforms.
Structurally, FN1 contains repeating type I, II, and III domains that mediate interactions with integrins (e.g., α5β1), collagen, heparin, and fibrin. The Arg-Gly-Asp (RGD) motif in the III10 domain is particularly crucial for cell binding. Recombinant FN1 retains these functional elements while offering advantages over native fibronectin, including batch-to-batch consistency, reduced immunogenicity, and customization (e.g., tag fusion for purification).
Its applications span cell culture (as a coating substrate to enhance attachment), tissue engineering (scaffold functionalization), and disease research. In cancer studies, FN1 overexpression correlates with metastasis and epithelial-mesenchymal transition. Recombinant FN1 fragments are also used to study wound healing mechanisms, fibrosis pathways (via TGF-β interactions), and microbial pathogenesis (e.g., bacterial adhesion). Therapeutic development leverages FN1-derived peptides for drug delivery systems or as anti-adhesive agents. The recombinant approach enables scalable production and domain-specific modifications, making it indispensable for both basic research and biotechnological applications requiring controlled extracellular matrix components.
×
