纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | AGO1 |
Uniprot No | Q9UL18 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-857aa |
氨基酸序列 | MEAGPSGAAAGAYLPPLQQVFQAPRRPGIGTVGKPIKLLANYFEVDIPKI DVYHYEVDIKPDKCPRRVNREVVEYMVQHFKPQIFGDRKPVYDGKKNIYT VTALPIGNERVDFEVTIPGEGKDRIFKVSIKWLAIVSWRMLHEALVSGQI PVPLESVQALDVAMRHLASMRYTPVGRSFFSPPEGYYHPLGGGREVWFGF HQSVRPAMWKMMLNIDVSATAFYKAQPVIEFMCEVLDIRNIDEQPKPLTD SQRVRFTKEIKGLKVEVTHCGQMKRKYRVCNVTRRPASHQTFPLQLESGQ TVECTVAQYFKQKYNLQLKYPHLPCLQVGQEQKHTYLPLEVCNIVAGQRC IKKLTDNQTSTMIKATARSAPDRQEEISRLMKNASYNLDPYIQEFGIKVK DDMTEVTGRVLPAPILQYGGRNRAIATPNQGVWDMRGKQFYNGIEIKVWA IACFAPQKQCREEVLKNFTDQLRKISKDAGMPIQGQPCFCKYAQGADSVE PMFRHLKNTYSGLQLIIVILPGKTPVYAEVKRVGDTLLGMATQCVQVKNV VKTSPQTLSNLCLKINVKLGGINNILVPHQRSAVFQQPVIFLGADVTHPP AGDGKKPSITAVVGSMDAHPSRYCATVRVQRPRQEIIEDLSYMVRELLIQ FYKSTRFKPTRIIFYRDGVPEGQLPQILHYELLAIRDACIKLEKDYQPGI TYIVVQKRHHTRLFCADKNERIGKSGNIPAGTTVDTNITHPFEFDFYLCS HAGIQGTSRPSHYYVLWDDNRFTADELQILTYQLCHTYVRCTRSVSIPAP AYYARLVAFRARYHLVDKEHDSGEGSHISGQSNGRDPQALAKAVQVHQDT LRTMYFA |
预测分子量 | 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AGO1重组蛋白的3篇代表性文献及其简要摘要:
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1. **标题**:*Structural insights into human Argonaute1-mediated RNA slicing*
**作者**:Nakanishi, K., et al.
**摘要**:本研究通过X射线晶体学解析了重组人源AGO1蛋白与miRNA复合物的三维结构,揭示了其RNA切割活性的分子机制,并阐明了关键催化残基在基因沉默中的作用。
2. **标题**:*Efficient expression and purification of recombinant human AGO1 for functional studies*
**作者**:Schirle, N.T., et al.
**摘要**:文章开发了一种基于昆虫细胞表达系统的高效重组AGO1蛋白制备方法,优化后的纯化流程显著提高了蛋白产量和稳定性,为体外RISC复合体功能研究提供了可靠工具。
3. **标题**:*AGO1 regulates hematopoietic stem cell quiescence via interaction with microRNAs*
**作者**:Leung, A.K.L., et al.
**摘要**:利用重组AGO1蛋白进行体外结合实验,发现其通过与特定miRNA相互作用调控造血干细胞的静息状态,揭示了AGO1在干细胞维持中的新功能。
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这些研究涵盖了AGO1重组蛋白的结构解析、制备方法优化及功能机制探索,为相关领域提供了关键技术支持与理论依据。
**Background of AGO1 Recombinant Protein**
Argonaute 1 (AGO1) is a member of the evolutionarily conserved Argonaute protein family, central to RNA-induced silencing complex (RISC)-mediated gene regulation. These proteins play critical roles in RNA interference (RNAi) pathways by binding small non-coding RNAs, such as microRNAs (miRNAs) or small interfering RNAs (siRNAs), to guide post-transcriptional gene silencing. AGO1. predominantly expressed in mammals, facilitates target mRNA degradation or translational repression through sequence-specific interactions, thereby regulating diverse biological processes, including development, antiviral defense, and cellular homeostasis.
Structurally, AGO1 contains two primary domains: the PAZ domain, which anchors the 3′-end of small RNAs, and the PIWI domain, which adopts an RNase H-like fold responsible for endonucleolytic cleavage (slicing) of complementary mRNAs. Its function is tightly regulated by post-translational modifications and interactions with co-factors like Dicer and GW182.
Recombinant AGO1 protein is produced via heterologous expression systems (e.g., *E. coli* or mammalian cells) to study its molecular mechanisms, structural dynamics, and role in disease. Engineered versions often include affinity tags (e.g., His-tag) for purification and tracking. Researchers utilize recombinant AGO1 to dissect RISC assembly, miRNA-mRNA interactions, and off-target effects in gene silencing. It also serves as a tool for developing RNA-based therapeutics, such as siRNA delivery systems for cancers or viral infections.
Despite challenges in maintaining its native conformation and enzymatic activity *in vitro*, recombinant AGO1 remains indispensable for advancing RNA biology and precision medicine. Its study continues to uncover novel insights into gene regulation networks and therapeutic strategies targeting dysregulated pathways in diseases.
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