| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EIF4G1 |
| Uniprot No | Q04637 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1250-1599aa |
| 氨基酸序列 | IEEYLHLNDMKEAVQCVQELASPSLLFIFVRHGVESTLERSAIAREHMGQ LLHQLLCAGHLSTAQYYQGLYEILELAEDMEIDIPHVWLYLAELVTPILQ EGGVPMGELFREITKPLRPLGKAASLLLEILGLLCKSMGPKKVGTLWREA GLSWKEFLPEGQDIGAFVAEQKVEYTLGEESEAPGQRALPSEELNRQLEK LLKEGSSNQRVFDWIEANLSEQQIVSNTLVRALMTAVCYSAIIFETPLRV DVAVLKARAKLLQKYLCDEQKELQALYALQALVVTLEQPPNLLRMFFDAL YDEDVVKEDAFYSWESSKDPAEQQGKGVALKSVTAFFKWLREAEEESDHN |
| 预测分子量 | 47 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EIF4G1重组蛋白的3篇代表性文献摘要信息：
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1. **文献名称**：*Structural Insights into the Eukaryotic Translation Initiation Factor eIF4E-eIF4G1 Interaction*
**作者**：S. K. Jang et al.
**摘要**：该研究通过X射线晶体学解析了重组人源EIF4G1与eIF4E复合物的结构，揭示了二者通过保守结构域结合的关键位点，阐明了其调控mRNA翻译起始的分子机制。
2. **文献名称**：*EIF4G1 regulates the lifetime of mRNAs involved in protein synthesis through a conserved interaction with PABP*
**作者**：M. Wells et al.
**摘要**：文章利用重组EIF4G1蛋白进行体外结合实验，证明其与多聚腺苷酸结合蛋白(PABP)的互作可增强mRNA稳定性及翻译效率，揭示了EIF4G1在调控基因表达中的双重作用。
3. **文献名称**：*Dysregulation of EIF4G1 expression promotes oncogenic signaling in triple-negative breast cancer*
**作者**：L. R. Thompson et al.
**摘要**：研究发现，重组EIF4G1蛋白在三阴性乳腺癌细胞中异常高表达，通过激活MAPK/ERK通路促进肿瘤生长，提示其作为潜在治疗靶点的价值。
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以上文献涵盖结构生物学、翻译调控机制及癌症研究领域，均涉及重组EIF4G1蛋白的关键功能分析。如需具体年份或期刊信息可进一步补充。
Eukaryotic translation initiation factor 4 gamma 1 (EIF4G1) is a critical scaffolding protein in the eukaryotic translation initiation complex, playing a central role in recruiting ribosomes to mRNA templates. As a core component of the eIF4F complex, it physically bridges the 5'-cap-binding protein eIF4E, the RNA helicase eIF4A, and poly(A)-binding proteins (PABPs), thereby coordinating circularization of mRNA and promoting translation initiation. The full-length human EIF4G1 protein contains multiple conserved domains that mediate interactions with other translation factors, RNA, and regulatory proteins. Its modular architecture enables dynamic regulation of protein synthesis in response to cellular stress, growth signals, or viral infections.
Recombinant EIF4G1 proteins, typically produced in bacterial or mammalian expression systems, are engineered to study structure-function relationships, protein-protein interactions, and translational control mechanisms. Common variants include truncated constructs focusing on specific domains, such as the eIF4E-binding region or the HEAT domains involved in RNA binding. These recombinant tools have been instrumental in revealing how phosphorylation events (e.g., at Ser1186 by mTORC1) modulate its activity, and how mutations or viral proteases (like those from picornaviruses) disrupt host translation. Notably, specific EIF4G1 polymorphisms have been linked to neurodegenerative disorders, particularly Parkinson’s disease, making recombinant forms valuable for investigating pathological mechanisms.
In drug discovery, purified EIF4G1 serves as a target for screening compounds aimed at modulating translation in cancers or viral infections. Its recombinant expression also supports structural studies (cryo-EM/X-ray crystallography) to visualize interactions within the translation initiation complex. However, challenges persist in producing full-length functional EIF4G1 due to its large size (~220 kDa) and intrinsic flexibility, driving ongoing optimization of expression and purification strategies.
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