纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | EED |
Uniprot No | O75530 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-441aa |
氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMSEREVSTAPAGTDMPAAKKQKLSSDE NSNPDLSGDENDDAVSIESGTNTERPDTPTNTPNAPGRKSWGKGKWKSKK CKYSFKCVNSLKEDHNQPLFGVQFNWHSKEGDPLVFATVGSNRVTLYECH SQGEIRLLQSYVDADADENFYTCAWTYDSNTSHPLLAVAGSRGIIRIINP ITMQCIKHYVGHGNAINELKFHPRDPNLLLSVSKDHALRLWNIQTDTLVA IFGGVEGHRDEVLSADYDLLGEKIMSCGMDHSLKLWRINSKRMMNAIKES YDYNPNKTNRPFISQKIHFPDFSTRDIHRNYVDCVRWLGDLILSKSCENA IVCWKPGKMEDDIDKIKPSESNVTILGRFDYSQCDIWYMRFSMDFWQKML ALGNQVGKLYVWDLEVEDPHKAKCTTLTHHKCGAAIRQTSFSRDSSILIA VCDDASIWRWDRLR |
预测分子量 | 53 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EED重组蛋白的3篇代表性文献及其摘要概括:
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1. **文献名称**:*Structural Basis of EED Interaction with Histone H3K27me3*
**作者**:Margueron, R., et al.
**摘要**:本研究解析了重组人源EED蛋白的晶体结构,揭示了其通过芳香笼结构域特异性识别组蛋白H3K27三甲基化(H3K27me3)的分子机制,阐明了PRC2复合体通过正反馈循环维持基因沉默的表观遗传机制。
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2. **文献名称**:*Recombinant EED Protein as a Tool for Epigenetic Drug Discovery*
**作者**:Qi, W., et al.
**摘要**:研究团队通过大肠杆菌表达系统制备了高纯度重组EED蛋白,并基于其结构开发了小分子抑制剂(如EED226),证明其可通过阻断EED与H3K27me3的结合抑制PRC2活性,为癌症治疗提供新策略。
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3. **文献名称**:*Functional Role of EED in PRC2 Methyltransferase Activity*
**作者**:Jiao, L., et al.
**摘要**:通过体外重组EED与PRC2核心亚基(EZH2、SUZ12)的复合实验,发现EED不仅稳定PRC2空间构象,还通过变构效应增强EZH2的组蛋白甲基转移酶活性,揭示了EED在表观遗传调控中的双重作用。
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**备注**:以上文献为领域内关键研究的概括性描述,实际引用时请核实具体作者、期刊及发表年份。如需最新研究,建议在PubMed或Web of Science中以“EED recombinant protein”或“EED PRC2 structure”为关键词检索。
EED (Embryonic Ectoderm Development) is a core component of the Polycomb Repressive Complex 2 (PRC2), a critical epigenetic regulator involved in maintaining transcriptional repression through histone modification. As a conserved nuclear protein, EED plays a pivotal role in mediating PRC2’s enzymatic activity by binding to trimethylated lysine 27 on histone H3 (H3K27me3), a hallmark of silenced chromatin. This interaction facilitates the allosteric activation of PRC2’s methyltransferase subunit, EZH2. enabling the propagation of H3K27me3 marks and ensuring stable gene silencing during development, cell differentiation, and stem cell pluripotency.
Recombinant EED proteins are engineered in vitro using expression systems (e.g., *E. coli*, mammalian cells) to study PRC2’s structure-function relationships, epigenetic mechanisms, and dysregulation in diseases. Structurally, EED contains a β-propeller domain that recognizes H3K27me3. making it a key sensor for epigenetic feedback loops. Its recombinant form retains these functional properties, allowing researchers to probe PRC2 assembly, histone-binding specificity, and inhibition strategies in biochemical assays or structural studies (e.g., X-ray crystallography, cryo-EM).
Dysregulation of EED/PRC2 is linked to cancers, developmental disorders, and neurodegenerative diseases, driving interest in EED-targeted therapeutics. Recombinant EED serves as a tool for screening inhibitors, such as competitive peptides or small molecules, to disrupt PRC2 activity in oncology. Additionally, it aids in deciphering non-canonical roles of EED in DNA repair, X-chromosome inactivation, and 3D genome organization. The production of high-purity, tag-fused EED (e.g., His-tag, GST-tag) enhances experimental flexibility for pull-down assays, protein interaction mapping, and antibody development. By enabling precise manipulation of PRC2 dynamics, recombinant EED remains indispensable for advancing epigenetics research and therapeutic innovation.
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