| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LFNG |
| Uniprot No | Q8NES3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-250aa |
| 氨基酸序列 | MTPGRCCLAADIQVETFIFTDGEDEALARHTGNVVITNCSAAHSRQALSCKMAVEYDRFIESGRKWFCHVDDDNYVNLRALLRLLASYPHTRDVYVGKPSLDRPIQAMERVSENKVRPVHFWFATGGAGFCISRGLALKMSPWASGGHFMNTAERIRLPDDCTIGYIVEALLGVPLIRSGLFHSHLENLQQVPTSELHEQVTLSYGMFENKRNAVHVKGPFSVEADPSRFRSIHCHLYPDTPWCPRTAIF |
| 预测分子量 | 55.2 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LFNG重组蛋白的3篇参考文献示例(注：文献为虚构示例，仅用于格式参考)：
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1. **文献名称**: *Lunatic Fringe (LFNG) regulates somitogenesis through Notch signaling modulation*
**作者**: Zhang Y, et al.
**摘要**: 研究利用重组LFNG蛋白在体外模型中验证其作为糖基转移酶的功能，证明其通过修饰Notch受体胞外结构域调控体节边界形成，并揭示其活性依赖特定金属离子。
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2. **文献名称**: *Structural basis of LFNG-mediated Notch1 O-fucosylation*
**作者**: Kovall RA, Haltiwanger RS.
**摘要**: 通过X射线晶体学解析重组人源LFNG蛋白与Notch1肽段的复合物结构，阐明其催化O-岩藻糖延伸的分子机制，为设计Notch通路抑制剂提供结构基础。
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3. **文献名称**: *LFNG overexpression inhibits T-cell leukemia progression in vivo*
**作者**: Kato H, et al.
**摘要**: 研究在小鼠模型中注射重组LFNG蛋白，发现其通过增强Notch信号拮抗作用抑制白血病细胞增殖，提示其作为潜在治疗分子的价值。
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如需真实文献，建议通过PubMed或Google Scholar检索关键词“LFNG recombinant protein”“Lunatic Fringe Notch”等。
**Background of LFNG Recombinant Protein**
LFNG (Lunatic Fringe) is a member of the Fringe family of glycosyltransferases, which are critical regulators of the Notch signaling pathway. This evolutionarily conserved pathway plays a central role in cell fate determination, tissue development, and homeostasis. Specifically, LFNG catalyzes the addition of *O*-fucose residues to epidermal growth factor-like (EGF) repeats of Notch receptors, modulating Notch-ligand interactions and ensuring precise spatial and temporal control of signaling activity. Dysregulation of LFNG has been implicated in developmental disorders, cancer, and other pathologies, underscoring its biological and clinical relevance.
Recombinant LFNG protein is produced using biotechnological platforms, such as *E. coli* or mammalian expression systems, to enable large-scale, high-purity yields for research and therapeutic applications. Its recombinant form retains enzymatic activity, allowing researchers to study Notch pathway dynamics, screen for modulators, or explore LFNG's role in diseases. For instance, aberrant LFNG expression correlates with T-cell acute lymphoblastic leukemia (T-ALL) and skeletal defects, making it a potential biomarker or therapeutic target.
Structurally, LFNG contains a conserved catalytic domain and substrate-binding regions critical for its interaction with Notch. Post-translational modifications, such as glycosylation, may influence its stability and function, necessitating tailored expression systems. Quality control assays (e.g., SDS-PAGE, enzymatic activity tests) ensure batch consistency.
In summary, LFNG recombinant protein serves as a vital tool for dissecting Notch signaling mechanisms and developing targeted therapies, bridging molecular biology with translational medicine.
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