| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FLII |
| Uniprot No | Q13045 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 495-827aa |
| 氨基酸序列 | VGQLPGLTIWQIENFVPVLVEEAFHGKFYEADCYIVLKTFLDDSGSLNWEIYYWIGGEATLDKKACSAIHAVNLRNYLGAECRTVREEMGDESEEFLQVFDNDISYIEGGTASGFYTVEDTHYVTRMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKNERKGKAEITLLVQGQELPEFWEALGGEPSEIKKHVPEDFWPPQPKLYKVGLGLGYLELPQINYKLSVEHKQRPKVELMPRMRLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELCGMLHRPRHATVSRSLEGTEAAAEQKLISEEDL |
| 预测分子量 | 44.6 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FLII重组蛋白的3篇参考文献及其摘要概括：
1. **标题**: "Recombinant Flightless-I protein enhances keratinocyte migration in vitro"
**作者**: Kopecki, Z., et al.
**摘要**: 研究报道了重组FLII蛋白在表皮细胞迁移中的作用，发现其通过调节肌动蛋白动态促进伤口愈合，为皮肤修复机制提供了新见解。
2. **标题**: "Structural and functional analysis of the Flightless-I protein reveals its role in actin remodeling"
**作者**: Lee, S.F., & Manser, E.
**摘要**: 通过重组FLII蛋白的结构解析，揭示了其与肌动蛋白结合的关键结构域，阐明了其在细胞骨架重组中的分子机制。
3. **标题**: "FLII expression modulates tumor cell invasion in colorectal cancer models"
**作者**: Smith, J.J., et al.
**摘要**: 实验证明重组FLII蛋白在结直肠癌细胞中过表达可抑制侵袭能力，提示其作为癌症治疗潜在靶点的可能性。
(注：上述文献为示例性质，实际引用时需核实具体文章信息。)
**Background of FLII Recombinant Protein**
FLII (Flightless I Homolog) is a multifunctional protein belonging to the gelsolin superfamily, conserved across eukaryotes. It plays critical roles in cytoskeletal remodeling, transcriptional regulation, and cellular signaling. Structurally, FLII contains leucine-rich repeats (LRRs) and gelsolin-like domains, enabling interactions with actin filaments and other proteins involved in motility, inflammation, and development. Its involvement in actin dynamics links FLII to processes like cell migration, cytokinesis, and intracellular trafficking.
Recombinant FLII protein is engineered using heterologous expression systems (e.g., *E. coli* or mammalian cells) to produce purified, functional FLII for research. This allows precise study of its biochemical properties, binding partners, and mechanisms. FLII's role in modulating actin polymerization and interacting with signaling pathways (e.g., Wnt/β-catenin, NF-κB) has implicated it in diseases, including cancer metastasis, fibrosis, and immune disorders. For instance, FLII overexpression in tumors may promote invasiveness, while its suppression in fibroblasts can attenuate fibrotic responses.
Researchers utilize recombinant FLII to explore its dual functions: as a cytoskeletal regulator and a nuclear coactivator. Studies also investigate its interplay with flightless family proteins and potential therapeutic targeting. The protein’s recombinant form ensures consistency in assays like pull-down experiments, enzyme-linked immunosorbent assays (ELISAs), or cell-based functional studies, advancing understanding of FLII’s pathophysiological roles and its viability as a biomarker or drug target.
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