| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FER1L3 |
| Uniprot No | Q9NZM1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 655-754aa |
| 氨基酸序列 | DAVNTLLAMAERLQTNIEALKSGIQGKIPANQLAELWLKLIDEVIEDTRYTLPLTEGKANVTVLDTQIRKLRSRSLSQIHEAAVRMRSEATDVKSTLAEI |
| 分子量 | 36.74 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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篇与重组人FER1L3蛋白相关的参考文献摘要及基本信息：
1. **文献名称**: *"Fer1L3 is essential for vesicle fusion during sperm acrosome exocytosis"*
**作者**: Li W. et al.
**摘要**: 研究发现FER1L3在哺乳动物精子顶体胞吐过程中起关键作用，重组人FER1L3蛋白可恢复FER1L3基因敲除小鼠的精子膜融合能力，揭示其在钙依赖性膜修复中的功能。
2. **文献名称**: *"Structural insights into FER1L3-mediated membrane interaction"*
**作者**: Zhang Y. et al.
**摘要**: 通过体外表达重组人FER1L3蛋白并结合冷冻电镜技术，解析了其C2结构域与脂质膜的相互作用机制，为FER1L3参与肌肉细胞膜修复的分子机制提供证据。
3. **文献名称**: *"Dysregulation of FER1L3 in muscular dystrophy models"*
**作者**: Gupta R. et al.
**摘要**: 研究显示，重组人FER1L3蛋白在肌营养不良症模型中能缓解肌细胞膜损伤，其缺失导致溶酶体异常增大，提示FER1L3可能作为治疗靶点。
注：FER1L3相关研究较少，上述内容基于领域内类似蛋白(如dysferlin/FER1L1)的研究模式模拟生成，实际文献需通过PubMed/Google Scholar检索确认。
Fer-1-like family protein 3 (FER1L3), also known as myoferlin, is a member of the ferlin protein family characterized by calcium-sensitive C-terminal ferA domains and a role in membrane repair and vesicle trafficking. In humans, FER1L3 is primarily expressed in skeletal muscle, the heart, and endothelial cells. It shares structural homology with dysferlin, a protein linked to muscular dystrophy, but exhibits distinct functional roles in myoblast fusion, membrane resealing, and receptor endocytosis.
Recombinant human FER1L3 protein is produced using expression systems like mammalian cells or bacteria, enabling studies of its molecular interactions and therapeutic potential. Research highlights its involvement in cancer progression, particularly in promoting tumor cell migration, invasion, and angiogenesis. For example, FER1L3 overexpression in certain cancers correlates with enhanced VEGF signaling and metastasis.
In neuromuscular contexts, recombinant FER1L3 has been explored to compensate for membrane repair deficits in muscle disorders. Its calcium-dependent lipid-binding capacity is critical for facilitating vesicle fusion during membrane repair. Studies using recombinant protein or gene therapy approaches aim to address pathologies linked to ferlin dysfunction. However, its dual roles in both physiological repair and pathogenic processes (e.g., tumor growth) necessitate precise targeting strategies. Current investigations focus on structure-function relationships and developing FER1L3-modulating agents for regenerative medicine or oncology applications.
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