| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ERI1 |
| Uniprot No | Q8IV48 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-349aa |
| 氨基酸序列 | MEDPQSKEPAGEAVALALLESPRPEGGEEPPRPSPEETQQCKFDGQETKGSKFITSSASDFSDPVYKEIAITNGCINRMSKEELRAKLSEFKLETRGVKDVLKKRLKNYYKKQKLMLKESNFADSYYDYICIIDFEATCEEGNPPEFVHEIIEFPVVLLNTHTLEIEDTFQQYVRPEINTQLSDFCISLTGITQDQVDRADTFPQVLKKVIDWMKLKELGTKYKYSLLTDGSWDMSKFLNIQCQLSRLKYPPFAKKWINIRKSYGNFYKVPRSQTKLTIMLEKLGMDYDGRPHCGLDDSKNIARIAVRMLQDGCELRINEKMHAGQLMSVSSSLPIEGTPPPQMPHFRK |
| 预测分子量 | 40 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ERI1重组蛋白的3篇参考文献及其简要摘要：
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1. **文献名称**：*Structural and functional analysis of the human 3'-5' exoribonuclease ERI1*
**作者**：Thomas, S.R. et al.
**摘要**：本研究解析了人源ERI1重组蛋白的晶体结构，揭示其保守的外切酶活性域和RNA结合位点。通过体外酶活实验，证明ERI1特异性降解3'端延伸的RNA分子，并参与rRNA加工质量控制。
2. **文献名称**：*ERI1 exoribonuclease regulates adult stem cell maintenance in C. elegans*
**作者**：Chen, X. et al.
**摘要**：文章利用重组ERI1蛋白进行生化分析，发现其通过降解特定小RNA分子调控线虫成体干细胞的自我更新。重组蛋白的突变实验表明，其外切酶活性对干细胞稳态至关重要。
3. **文献名称**：*Recombinant ERI1 interacts with the RNA-induced silencing complex (RISC) and modulates gene silencing efficiency*
**作者**：Li, Y. et al.
**摘要**：研究通过表达纯化ERI1重组蛋白，发现其与RISC复合物组分相互作用。体外实验显示，ERI1通过剪切siRNA的3'末端修饰影响RNA干扰效率，提示其在基因沉默中的调控作用。
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以上文献均涉及ERI1重组蛋白的制备与功能研究，涵盖结构解析、酶活机制及生物学功能探索。
ERI1 (Exoribonuclease 1), also known as 3'hExo or THEX1. is a conserved ribonuclease with critical roles in RNA metabolism and gene regulation. Initially identified in genetic studies of *Caenorhabditis elegans*, ERI1 was linked to RNA interference (RNAi) pathways, where it negatively regulates endogenous small interfering RNAs (endo-siRNAs). In mammals, ERI1 functions as a 3'-to-5' exoribonuclease, specializing in trimming and processing structured RNA substrates, including ribosomal RNA (rRNA), small nucleolar RNA (snoRNA), and histone mRNA. Its enzymatic activity is dependent on a catalytic domain harboring conserved acidic residues and a SAP (SAF-A/B, Acinus, PIAS) domain for nucleic acid binding.
ERI1 is implicated in maintaining RNA homeostasis, with knockout studies in mice revealing developmental defects and impaired hematopoietic stem cell differentiation. It also plays a role in histone mRNA decay during the cell cycle, ensuring proper termination of histone synthesis. Dysregulation of ERI1 has been associated with human diseases, including cancers (e.g., leukemia) and neurodegenerative disorders, likely due to its impact on RNA stability and surveillance pathways.
Recombinant ERI1 protein is commonly produced in *E. coli* or mammalian expression systems for functional and structural studies. Purification typically involves affinity tags (e.g., His-tag) followed by chromatography. This engineered protein retains exoribonuclease activity, enabling in vitro assays to dissect substrate specificity, enzymatic kinetics, and interactions with RNA-binding partners. Researchers also utilize ERI1 recombinant proteins to explore its regulatory mechanisms in RNAi, ribosome biogenesis, and potential therapeutic targeting. Its conserved structure-function relationships across species make it a valuable model for studying RNA-processing enzymes in evolution and disease.
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