| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MFNG |
| Uniprot No | O00587 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-321aa |
| 氨基酸序列 | MQCRLPRGLAGALLTLLCMGLLCLRYHLNLSPQRVQGTPELSQPNPGPPKLQLHDVFIAVKTTRAFHRLRLELLLDTWVSRTREQTFVFTDSPDKGLQERLGSHLVVTNCSAEHSHPALSCKMAAEFDTFLASGLRWFCHVDDDNYVNPRALLQLLRAFPLARDVYVGRPSLNRPIHASEPQPHNRTRLVQFWFATGGAGFCINRKLALKMAPWASGSRFMDTSALIRLPDDCTMGYIIECKLGGRLQPSPLFHSHLETLQLLRTAQLPEQVTLSYGVFEGKLNVIKLQGPFSPEEDPSRFRSLHCLLYPDTPWCPQLGAR |
| 预测分子量 | 36,2 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MFNG(Manic Fringe)重组蛋白研究的3篇代表性文献摘要示例(注：内容为模拟概括，非真实文献)：
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1. **文献名称**：Structural analysis of Manic Fringe reveals key residues for Notch signaling regulation
**作者**：Chen L, et al.
**摘要**：本研究通过重组表达人源MFNG蛋白，利用X射线晶体学解析了其三维结构，揭示了其岩藻糖基转移酶活性中心的关键氨基酸残基，并验证了其对Jagged1-Notch相互作用的调控机制，为靶向Notch通路的药物设计提供依据。
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2. **文献名称**：Recombinant MFNG enhances hematopoietic stem cell differentiation in vitro
**作者**：Wang Y, et al.
**摘要**：通过哺乳动物细胞系统表达纯化MFNG重组蛋白，证明其在体外可促进造血干细胞向T细胞谱系分化，并依赖Notch受体配体结合域的糖基化修饰。该研究为免疫细胞疗法开发提供了实验支持。
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3. **文献名称**：MFNG overexpression correlates with poor prognosis in breast cancer
**作者**：Rodriguez S, et al.
**摘要**：通过重组MFNG蛋白处理乳腺癌细胞系，发现其通过增强Notch1信号通路激活上皮-间质转化(EMT)，促进肿瘤侵袭转移。临床数据分析显示MFNG高表达与患者生存率负相关。
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此类研究多发表于《Journal of Biological Chemistry》《Cell Reports》《Oncogene》等期刊，实际文献需通过PubMed或Google Scholar检索关键词"recombinant MFNG protein" "Manic Fringe Notch"获取。
**Background of MFNG Recombinant Protein**
The Manic Fringe (MFNG) recombinant protein is a engineered version of the human MFNG glycosyltransferase, a key regulator of the evolutionarily conserved Notch signaling pathway. MFNG belongs to the Fringe family of β-1.3-N-acetylglucosaminyltransferases, which modulate Notch receptor activity by glycosylating extracellular epidermal growth factor (EGF)-like repeats. Specifically, MFNG catalyzes the addition of N-acetylglucosamine (GlcNAc) to O-fucose residues on Notch receptors, fine-tuning Notch-ligand interactions and downstream signaling. This post-translational modification is critical for cell fate determination, tissue development, and homeostasis, with dysregulation linked to cancers, cardiovascular disorders, and developmental anomalies.
Recombinant MFNG is typically produced in mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper folding and post-translational modifications. The purified protein retains enzymatic activity, enabling researchers to study its role in Notch pathway regulation *in vitro* or *in vivo*. Its applications span structural studies, enzymatic assays, and functional investigations into developmental biology, stem cell differentiation, and tumorigenesis. For instance, MFNG overexpression or inhibition models help elucidate its context-dependent roles as either an oncogene or tumor suppressor in cancers like T-cell acute lymphoblastic leukemia (T-ALL) and breast cancer.
Additionally, MFNG recombinant protein serves as a tool for drug discovery, particularly in designing glycosylation-targeted therapies. Its structural characterization aids in mapping substrate-binding domains and developing small-molecule inhibitors. As Notch signaling intersects with multiple pathways (e.g., Wnt, Hedgehog), MFNG reagents are vital for unraveling cross-talk mechanisms in disease models. Overall, MFNG recombinant protein bridges biochemical, cellular, and translational research, offering insights into developmental defects and therapeutic strategies for Notch-related pathologies.
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