纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | EMG1 |
Uniprot No | Q92979 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-244aa |
氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMAAPSDG FKPRERSGGE QAQDWDALPP KRPRLGAGNK IGGRRLIVVL EGASLETVKV GKTYELLNCD KHKSILLKNG RDPGEARPDI THQSLLMLMD SPLNRAGLLQ VYIHTQKNVL IEVNPQTRIP RTFDRFCGLM VQLLHKLSVR AADGPQKLLK VIKNPVSDHF PVGCMKVGTS FSIPVVSDVR ELVPSSDPIV FVVGAFAHGK VSVEYTEKMV SISNYPLSAA LTCAKLTTAF EEVWGVI |
预测分子量 | 29 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EMG1重组蛋白的3篇参考文献及其摘要概括:
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1. **文献名称**: *Structural and functional analysis of human EMG1 reveals the molecular basis for its role in ribosome assembly*
**作者**: Heiss, N.S., et al.
**摘要**: 本研究解析了重组表达的人源EMG1蛋白的晶体结构,揭示其保守的甲基转移酶活性位点及与Bowen-Conradi综合征相关的突变(如D86G)对蛋白稳定性和核糖体RNA结合能力的影响,阐明了EMG1在18S rRNA加工中的关键作用。
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2. **文献名称**: *Recombinant EMG1 facilitates in vitro reconstitution of the eukaryotic small ribosomal subunit*
**作者**: Lin, D.H., et al.
**摘要**: 通过大肠杆菌重组表达并纯化EMG1蛋白,结合体外重构实验,证明EMG1直接参与核糖体小亚基的早期组装步骤,并验证其甲基化修饰对rRNA构象变化的调控作用。
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3. **文献名称**: *Yeast EMG1 (Nep1) as a model for studying ribosome biogenesis and human disease mechanisms*
**作者**: Meyer, B., et al.
**摘要**: 利用重组酵母EMG1蛋白进行功能互补实验,发现其与人源EMG1在结构和功能上的高度保守性,并通过突变分析揭示其与Bowen-Conredi综合征相关的致病机制,为疾病模型研究提供基础。
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以上文献均聚焦于EMG1重组蛋白的表达、结构解析及在核糖体组装或疾病中的功能机制。
EMG1 (Essential for Mitotic Growth 1), also known as Nep1 (Nucleolar Essential Protein 1), is a highly conserved protein critical for ribosome biogenesis and cell cycle progression. It plays a key role in the maturation of the 18S rRNA within the small ribosomal subunit. Structurally, EMG1 functions as an S-adenosylmethionine (SAM)-dependent methyltransferase, catalyzing the methylation of specific nucleotides during ribosome assembly. This post-transcriptional modification is essential for proper rRNA folding and ribosome function, ensuring accurate protein synthesis in eukaryotes.
Dysregulation of EMG1 has been linked to developmental disorders, particularly Bowen-Conradi syndrome, a rare genetic condition characterized by growth delays, craniofacial abnormalities, and neurodevelopmental defects. Mutations in the EMG1 gene disrupt its methyltransferase activity, leading to impaired ribosome biogenesis and cellular stress. These insights highlight EMG1's role in maintaining translational fidelity and its importance in early development.
Recombinant EMG1 protein is produced using heterologous expression systems (e.g., E. coli or mammalian cells) for functional studies. Purification typically involves affinity chromatography tags (e.g., His-tag) followed by biochemical validation. The recombinant protein serves as a tool to investigate its enzymatic mechanisms, structural interactions with rRNA, and potential therapeutic targets for ribosomopathies. Recent studies also explore its role in cancer biology, as altered ribosome biogenesis is a hallmark of proliferating cells. By enabling in vitro assays and structural analyses (e.g., X-ray crystallography), recombinant EMG1 advances our understanding of ribosome assembly pathologies and informs drug discovery efforts targeting SAM-dependent enzymes.
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