纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | FMR1 |
Uniprot No | Q8IXW7 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-297aa |
氨基酸序列 | MEELVVEVRGSNGAFYKAFVKDVHEDSITVAFENNWQPDRQIPFHDVRFP PPVGYNKDINESDEVEVYSRANEKEPCCWWLAKVRMIKGEFYVIEYAACD ATYNEIVTIERLRSVNPNKPATKDTFHKIKLDVPEDLRQMCAKEAAHKDF KKAVGAFSVTYDPENYQLVILSINEVTSKRAHMLIDMHFRSLRTKLSLIM RNEEASKQLESSRQLASRFHEQFIVREDLMGLAIGTHGANIQQARKVPGV TAIDLDEDTCTFHIYGEDQDAVKKARSFLEFAEDVIQVPRNLVGLKI |
预测分子量 | 58 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3篇关于FMR1重组蛋白的经典及近期文献概览:
1. **文献名称**:*Production of Recombinant Fragile X Mental Retardation Protein Isoforms and Their Detection in Cell Extracts*
**作者**:K. D’Hulst et al.
**摘要**:该研究描述了在大肠杆菌中高效表达并纯化人源FMR1重组蛋白(FMRP)不同异构体的方法,验证了重组蛋白的RNA结合活性,并建立了针对细胞提取物中FMRP的定量检测技术。
2. **文献名称**:*Structural Insights into the Recognition of Histone H3 by the FMR1 Recombinant Protein*
**作者**:S. Alpatov et al.
**摘要**:通过X射线晶体学解析FMR1重组蛋白与组蛋白H3的复合物结构,揭示了FMRP通过其N端结构域特异性识别组蛋白H3甲基化修饰的分子机制,为脆性X综合征的表观遗传调控研究提供依据。
3. **文献名称**:*Functional Characterization of FMR1 Recombinant Protein in Drosophila Synaptic Plasticity Models*
**作者**:L. Zhang et al.
**摘要**:利用果蝇神经系统模型,证明重组人源FMRP蛋白可挽救fmr1基因缺失突变体的突触可塑性缺陷,表明重组蛋白在跨物种功能研究中具有活性,支持FMRP在神经发育中的保守作用。
注:以上文献为示例性质,实际引用时建议通过PubMed或期刊数据库核对最新研究。若需具体文献DOI或补充领域方向(如蛋白互作、疾病机制),可进一步说明。
The FMR1 gene, located on the X chromosome, encodes the fragile X mental retardation protein (FMRP), an RNA-binding protein critical for neuronal development, synaptic plasticity, and cognitive function. Mutations in FMR1. particularly a CGG triplet repeat expansion in the 5' untranslated region, are linked to fragile X syndrome (FXS), the most common inherited cause of intellectual disability. Full mutations (>200 CGG repeats) lead to gene silencing and loss of FMRP, disrupting mRNA translation, transport, and stability in neurons. Premutation carriers (55–200 repeats) may develop FMR1-related disorders, including fragile X-associated tremor/ataxia syndrome (FXTAS) and primary ovarian insufficiency (FXPOI), due to toxic RNA gain-of-function or reduced FMRP levels.
Recombinant FMR1 protein, produced via heterologous expression systems (e.g., bacterial, yeast, or mammalian cells), enables mechanistic studies of FMRP’s roles in neurodevelopment and disease. Its production allows large-scale analysis of FMRP’s structure, RNA/DNA-binding domains, and interactions with neuronal targets like ion channels and synaptic proteins. Researchers use recombinant FMRP to model FXS pathophysiology, screen therapeutic compounds, and develop protein replacement strategies. Challenges include preserving post-translational modifications (e.g., phosphorylation) critical for function and mimicking native cellular localization. Current studies focus on leveraging recombinant FMRP to restore neuronal translation regulation, correct synaptic defects, or target downstream pathways in FXS. Advances in protein engineering and delivery systems may enhance its therapeutic potential for fragile X-related disorders.
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