| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FBLIM1 |
| Uniprot No | Q8WUP2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-373aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMASKPEKRVASSVFITLAPPRRDVAVA EEVRQAVCEARRGRPWEAPAPMKTPEAGLAGRPSPWTTPGRAAATVPAAP MQLFNGGCPPPPPVLDGEDVLPDLDLLPPPPPPPPVLLPSEEEAPAPMGA SLIADLEQLHLSPPPPPPQAPAEGPSVQPGPLRPMEEELPPPPAEPVEKG ASTDICAFCHKTVSPRELAVEAMKRQYHAQCFTCRTCRRQLAGQSFYQKD GRPLCEPCYQDTLERCGKCGEVVRDHIIRALGQAFHPSCFTCVTCARCIG DESFALGSQNEVYCLDDFYRKFAPVCSICENPIIPRDGKDAFKIECMGRN FHENCYRCEDCRILLSVEPTDQGCYPLNNHLFCKPCHVKRSAAGCC |
| 预测分子量 | 43 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FBLIM1重组蛋白的3篇示例参考文献(内容为模拟概括，建议通过学术数据库验证具体信息)：
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1. **文献名称**: *FBLIM1 regulates osteoblast differentiation via NF-κB signaling*
**作者**: Zhang L, et al.
**摘要**: 研究通过重组FBLIM1蛋白探究其在成骨细胞分化中的作用，发现FBLIM1通过抑制NF-κB通路促进骨形成，为骨质疏松治疗提供潜在靶点。
2. **文献名称**: *Recombinant FBLIM1 suppresses synovial inflammation in rheumatoid arthritis models*
**作者**: Tanaka K, et al.
**摘要**: 利用重组FBLIM1蛋白处理类风湿关节炎小鼠模型，发现其通过调控整合素信号通路减少滑膜炎症和关节破坏，提示其治疗应用价值。
3. **文献名称**: *FBLIM1 interacts with filamin A to modulate cancer cell migration*
**作者**: Chen H, et al.
**摘要**: 通过体外实验证明重组FBLIM1蛋白与Filamin A结合，抑制肿瘤细胞迁移和侵袭，揭示其在癌症转移中的抑制作用机制。
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建议通过PubMed、Web of Science或Google Scholar以关键词“FBLIM1 recombinant protein”或“FBLIM1 function”检索最新文献获取准确信息。
**Background of FBLIM1 Recombinant Protein**
FBLIM1 (Filamin-Binding LIM Protein 1), also known as migfilin, is a cytoskeletal protein that plays a critical role in cell adhesion, migration, and mechanotransduction. It acts as an adaptor molecule, linking the actin cytoskeleton to the extracellular matrix (ECM) by interacting with filamin (a key actin crosslinking protein) and integrins (transmembrane receptors mediating cell-ECM interactions). The protein contains a LIM domain, which is crucial for its localization and function in focal adhesions—specialized sites where cells attach to the ECM.
FBLIM1 is implicated in regulating cell morphology, signaling pathways, and tissue homeostasis. Studies highlight its involvement in inflammatory diseases, such as rheumatoid arthritis and osteoarthritis, where altered FBLIM1 expression correlates with synovial fibroblast activation and cartilage degradation. In cancer, FBLIM1 exhibits dual roles, acting as a tumor suppressor by inhibiting cell invasion in some contexts or promoting metastasis in others, depending on the cellular environment and post-translational modifications.
Recombinant FBLIM1 protein is engineered for *in vitro* and *in vivo* studies to dissect its molecular interactions, structural features, and therapeutic potential. Produced via heterologous expression systems (e.g., *E. coli* or mammalian cells), it retains functional domains required for binding partners like filamin and integrins. Researchers utilize this tool to explore FBLIM1’s role in cell signaling (e.g., TGF-β, Wnt pathways), mechanobiology, and disease mechanisms. Its application extends to developing biomarkers or targeted therapies for conditions involving dysregulated cell adhesion, such as fibrosis, cancer metastasis, and chronic inflammatory disorders.
Overall, FBLIM1 recombinant protein serves as a vital resource for advancing understanding of cell-ECM communication and its pathological disruptions.
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