| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FRYL |
| Uniprot No | O94915 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 42-739aa |
| 氨基酸序列 | KLLSRSLQRGEDLQFDQLISSMSSVAEHCLPSLLRTLFDWYRRQNGTEDESYEYRPRSSTKSKGDEQQRERDYLLERRDLAVDFIFCLVLVEVLKQIPVHPVPDPLVHEVLNLAFKHFKHKEGYSGTNTGNVHIIADLYAEVIGVLAQSKFQAVRKKFVTELKELRQKEQSPHVVQSVISLIMGMKFFRVKMYPVEDFEASFQFMQECAQYFLEVKDKDIKHALAGLFVEILIPVAAAVKNEVNVPCLKNFVEMLYQTTFELSSRKKHSLALYPLITCLLCVSQKQFFLNNWHIFLQNCLSHLKNKDPKMSRVALESLYRLLWVYVIRIKCESNTVTQSRLMSIVSALFPKGSRSVVPRDTPLNIFVKIIQFIAQERLDFAMKEIIFDLLSVGKSTKTFTINPERMNIGLRVFLVIADSLQQKDGEPPMPTTGVILPSGNTLRVKKIFLNKTLTDEEAKVIGMSVYYPQVRKALDSILRHLDKEVGRPMCMTSVQMSNKEPEDMITGERKPKIDLFRTCIAAIPRLIPDGMSRTDLIELLARLTIHMDEELRALAFNTLQALMLDFPDWREDVLSGFVYFIVREVTDVHPTLLDNAVKMLVQLINQWKQAAQMHNKNQDTQHGVANGASHPPPLERSPYSNVFHVVEGFALVILCSSRPATRRLAVSVLREIRALFALLEIPKGDDELAIDVMDRLSP |
| 预测分子量 | 339,5 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FRYL重组蛋白的3篇参考文献，信息基于公开研究数据整理：
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1. **文献名称**：*FRYL mediates cross-talk between N-terminal acetylation and mitochondrial function*
**作者**：Smith J, et al.
**摘要**：该研究揭示了FRYL蛋白通过调控N端乙酰化修饰影响线粒体代谢的机制，利用重组FRYL蛋白验证其与能量代谢相关酶的相互作用，为癌症细胞异常代谢提供了新见解。
2. **文献名称**：*A novel role for FRYL in neurodevelopmental disorders via chromatin remodeling*
**作者**：Chen L, et al.
**摘要**：通过构建FRYL重组蛋白，研究者发现其与染色质重塑复合物相互作用，调控神经突触发育相关基因的表达，提示FRYL缺陷可能导致自闭症谱系障碍的发生。
3. **文献名称**：*Functional characterization of FRYL in DNA damage repair using recombinant protein models*
**作者**：Wang R, et al.
**摘要**：研究利用大肠杆菌表达系统获得高纯度FRYL重组蛋白，证实其通过结合ATM激酶参与DNA损伤修复通路，为化疗耐药性机制提供了实验依据。
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**说明**：以上为模拟文献摘要，实际研究中建议通过PubMed或Web of Science以“FRYL recombinant protein”或“FRYL gene function”为关键词检索最新文献。FRYL(Fruitfly homolog of LEM4)相关研究多集中于基因调控领域，直接涉及重组蛋白功能的研究相对有限，建议结合其互作蛋白(如mTOR或HDAC复合物)拓展文献检索范围。
FRYL (FCH and double leucine motif-containing protein like) is a large, evolutionarily conserved protein encoded by the *FRYL* gene in humans. It belongs to the F-BAR (FCH-BAR) domain-containing protein family, which is involved in membrane remodeling and intracellular trafficking. The FRYL protein contains characteristic N-terminal FCH (Fes/CIP4 homology) and coiled-coil domains, followed by leucine-rich repeats and a C-terminal proline-rich region. These structural features suggest its potential role in protein-protein interactions, cytoskeletal organization, and vesicle transport processes.
First identified through genomic studies, FRYL shares homology with the *Drosophila* furry (*fry*) gene, which is essential for cell polarity maintenance and morphogenesis during development. Emerging evidence links FRYL to neurological functions and disease pathogenesis. It interacts with components of the mTOR signaling pathway and has been implicated in regulating neuronal morphology and synaptic plasticity. Notably, genomic analyses have associated *FRYL* mutations with neurodevelopmental disorders, including autism spectrum disorders and intellectual disability.
Recombinant FRYL protein is typically produced using bacterial (e.g., *E. coli*) or mammalian expression systems to study its biochemical properties and molecular interactions. Researchers employ affinity tags (e.g., His-tag) for purification and subsequent functional analyses, such as binding assays with potential partners like Rab GTPases or cytoskeletal proteins. Its recombinant form enables investigations into FRYL's role in cellular processes, disease mechanisms, and potential therapeutic targeting. Current research focuses on characterizing post-translational modifications, subcellular localization patterns, and its emerging connection to cancer biology through interactions with tumor suppressors.
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