| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RFNG |
| Uniprot No | Q9Y644 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-331aa |
| 氨基酸序列 | MSRARGALCRACLALAAALAALLLLPLPLPRAPAPARTPAPAPRAPPSRPAAPSLRPDDVFIAVKTTRKNHGPRLRLLLRTWISRARQQTFIFTDGDDPELELQGGDRVINTNCSAVRTRQALCCKMSVEYDKFIESGRKWFCHVDDDNYVNARSLLHLLSSFSPSQDVYLGRPSLDHPIEATERVQGGRTVTTVKFWFATGGAGFCLSRGLALKMSPWASLGSFMSTAEQVRLPDDCTVGYIVEGLLGARLLHSPLFHSHLENLQRLPPDTLLQQVTLSHGGPENPHNVVNVAGGFSLHQDPTRFKSIHCLLYPDTDWCPRQKQGAPTSR |
| 预测分子量 | 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RFNG(可能与重组蛋白或相关功能研究相关)的3篇参考文献示例(注：RFNG可能指特定领域重组蛋白，部分内容为模拟文献)：
1. **文献名称**: "Functional characterization of RFNG recombinant protein in Notch signaling regulation"
**作者**: Zhang L, et al.
**摘要**: 研究通过大肠杆菌表达系统成功表达并纯化RFNG重组蛋白，证实其作为糖基转移酶在Notch信号通路中修饰配体的关键作用，揭示了RFNG对细胞分化的分子调控机制。
2. **文献名称**: "Structural analysis of RFNG protein and its interaction with Delta-like ligands"
**作者**: Kim S, Patel R.
**摘要**: 通过X射线晶体学解析RFNG重组蛋白的三维结构，发现其活性位点对底物识别至关重要，并证明其与Delta-like配体的结合可增强Notch受体活化，为靶向治疗提供结构基础。
3. **文献名称**: "RFNG recombinant protein enhances neuronal regeneration in vitro"
**作者**: Gomez M, et al.
**摘要**: 利用哺乳动物细胞表达的RFNG重组蛋白处理神经干细胞，发现其显著促进轴突生长和突触形成，表明其在神经损伤修复中的潜在应用价值。
(注：以上文献为示例，实际研究中请根据具体方向检索真实数据库如PubMed或Google Scholar。)
Radial Fringe (RFNG) is a member of the Fringe family of β-1.3-N-acetylglucosaminyltransferases, which are critical modulators of the Notch signaling pathway. Initially identified in Drosophila, Fringe proteins (including LFNG, MFNG, and RFNG in mammals) regulate cell-cell communication by glycosylating Notch receptors, fine-tuning their interactions with ligands like Delta and Jagged. RFNG specifically modifies O-fucose residues on epidermal growth factor (EGF)-like repeats of Notch extracellular domains, influencing ligand selectivity and signal strength. This post-translational modification is essential for boundary formation, cell fate determination, and tissue patterning during embryonic development, particularly in neurogenesis, somitogenesis, and limb development.
Recombinant RFNG protein, typically produced in mammalian or insect expression systems, retains enzymatic activity for experimental applications. Its production enables detailed biochemical characterization of Fringe-Notch interactions and facilitates studies on developmental disorders linked to Notch dysregulation, such as congenital scoliosis or Alagille syndrome. Researchers utilize recombinant RFNG in vitro to reconstitute Notch glycosylation events, investigate structure-function relationships, and screen potential therapeutic modulators. Recent advances in structural biology have leveraged recombinant RFNG to resolve 3D conformations of glycosylated Notch complexes, providing mechanistic insights into how subtle glycan modifications dictate cellular signaling outcomes. The protein's role in cancer biology is also under exploration, as aberrant Notch activity contributes to tumor progression in multiple malignancies.
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