| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EIF3I |
| Uniprot No | Q13347 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-325aa |
| 氨基酸序列 | MKPILLQGHERSITQIKYNREGDLLFTVAKDPIVNVWYSVNGERLGTYMGHTGAVWCVDADWDTKHVLTGSADNSCRLWDCETGKQLALLKTNSAVRTCGFDFGGNIIMFSTDKQMGYQCFVSFFDLRDPSQIDNNEPYMKIPCNDSKITSAVWGPLGECIIAGHESGELNQYSAKSGEVLVNVKEHSRQINDIQLSRDMTMFVTASKDNTAKLFDSTTLEHQKTFRTERPVNSAALSPNYDHVVLGGGQEAMDVTTTSTRIGKFEARFFHLAFEEEFGRVKGHFGPINSVAFHPDGKSYSSGGEDGYVRIHYFDPQYFEFEFEA |
| 预测分子量 | 39 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EIF3I重组蛋白的3篇参考文献示例(文献信息为模拟，仅供格式参考)：
1. **标题**：*EIF3I promotes tumor progression by regulating cell cycle via mTOR signaling*
**作者**：Chen L, et al.
**摘要**：研究揭示了EIF3I在结直肠癌中过表达，通过重组蛋白体外实验证实其激活mTOR通路并加速G1/S期转化，促进肿瘤细胞增殖和转移。
2. **标题**：*Crystal structure of human EIF3I reveals a conserved RNA-binding domain*
**作者**：Gupta R, et al.
**摘要**：利用重组EIF3I蛋白解析其晶体结构，发现其C端具有保守的RNA结合基序，为理解真核翻译起始复合物组装机制提供结构基础。
3. **标题**：*EIF3I interacts with hepatitis C virus core protein to modulate viral replication*
**作者**：Wang Y, et al.
**摘要**：通过重组EIF3I与HCV核心蛋白的共沉淀实验，证明两者直接结合，且EIF3I敲低显著抑制病毒复制，提示其在丙肝感染中的调控作用。
4. **标题**：*EIF3I regulates selective mRNA translation in stem cell pluripotency*
**作者**：Kim S, et al.
**摘要**：利用重组EIF3I蛋白进行核糖体分析，发现其通过优先翻译多能性相关基因(如OCT4)维持胚胎干细胞的未分化状态。
**Background of EIF3I Recombinant Protein**
Eukaryotic Initiation Factor 3 subunit I (EIF3I) is a critical component of the EIF3 complex, a multiprotein assembly essential for initiating translation in eukaryotes. The EIF3 complex plays a central role in ribosome recruitment to mRNA, scanning for the start codon, and regulating the assembly of the 48S preinitiation complex. Among its 13 subunits, EIF3I (also known as EIF3S2 or TRIP1) contributes to structural stability and functional coordination of the complex. It interacts with other EIF3 subunits, such as EIF3A and EIF3B, and participates in binding ribosomal subunits and mRNA.
EIF3I’s recombinant form is engineered for in vitro studies to dissect its molecular interactions and mechanisms in translation regulation. Recombinant EIF3I is typically expressed in prokaryotic (e.g., *E. coli*) or eukaryotic systems (e.g., HEK293 cells) with affinity tags (e.g., His-tag) for purification. Its production enables biochemical assays, structural analyses (e.g., cryo-EM), and exploration of its role in diseases. Notably, dysregulation of EIF3I has been linked to cancers, including breast and prostate cancer, where its overexpression correlates with tumor progression and poor prognosis.
Research on recombinant EIF3I also extends to understanding viral infections, as some viruses hijack the host translation machinery via EIF3 interactions. Additionally, it serves as a tool for screening small-molecule inhibitors targeting translation initiation in cancer therapeutics. Challenges in working with recombinant EIF3I include maintaining its native conformation and post-translational modifications, which are crucial for functional studies. Despite these hurdles, EIF3I remains a vital reagent for unraveling translation mechanisms and developing targeted therapies.
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