| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EIF1 |
| Uniprot No | P41567 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-113aa |
| 氨基酸序列 | MSAIQNLHSFDPFADASKGDDLLPAGTEDYIHIRIQQRNGRKTLTTVQGIADDYDKKKLVKAFKKKFACNGTVIEHPEYGEVIQLQGDQRKNICQFLVEIGLAKDDQLKVHGF |
| 预测分子量 | 39.7kDa |
| 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EIF1重组蛋白的模拟参考文献示例(仅供参考，非真实文献)：
1. **《重组EIF1蛋白在大肠杆菌中的高效表达与纯化》**
*作者：Smith A, et al.*
摘要：研究利用大肠杆菌表达系统成功克隆并高效表达EIF1重组蛋白，通过亲和层析纯化获得高纯度蛋白，为后续功能研究奠定基础。
2. **《EIF1的晶体结构揭示其在翻译起始中的构象变化机制》**
*作者：Zhang L, et al.*
摘要：通过X射线晶体学解析EIF1重组蛋白的三维结构，发现其与核糖体小亚基结合时的构象动态变化，阐明其对起始密码子选择的关键作用。
3. **《EIF1功能缺失突变体对真核翻译起始复合体组装的影响》**
*作者：Wang Y, et al.*
摘要：利用重组EIF1蛋白构建功能缺失突变体，证明其通过破坏起始因子相互作用导致翻译起始复合体组装异常，影响蛋白质合成效率。
4. **《EIF1重组蛋白在肝癌细胞异常翻译调控中的功能研究》**
*作者：Tanaka K, et al.*
摘要：体外实验显示，重组EIF1蛋白可抑制肝癌细胞中异常翻译通路的激活，提示其作为潜在肿瘤治疗靶点的可能性。
注：以上为模拟文献，实际研究中建议通过PubMed或Web of Science等数据库检索真实论文。
Eukaryotic Initiation Factor 1 (EIF1) is a critical regulatory protein involved in the initiation phase of eukaryotic translation. As a core component of the 43S pre-initiation complex, EIF1 plays a pivotal role in ensuring the accuracy of start codon selection during ribosome scanning of mRNA. It binds to the 40S ribosomal subunit and stabilizes an "open" conformation of the complex, allowing proper inspection of potential initiation codons. This function prevents premature ribosomal subunit association and reduces translation errors caused by non-AUG codons or upstream open reading frames (uORFs).
Structurally, EIF1 is a small, highly conserved protein (~12 kDa) containing a zinc-binding domain essential for its interactions with other initiation factors. Its molecular mechanism involves coordinating with EIF1A to regulate the stringency of start codon recognition. When the correct AUG codon is identified, EIF1 dissociates from the ribosome, triggering structural rearrangements that promote subunit joining and transition to elongation.
Recombinant EIF1 proteins are typically produced using bacterial expression systems (e.g., *E. coli*) with affinity tags for purification. These engineered proteins enable detailed biochemical studies, including X-ray crystallography and cryo-EM analyses that have revealed atomic-level insights into translation initiation mechanisms. Researchers utilize recombinant EIF1 to investigate mutations linked to developmental disorders and cancer, particularly those affecting its interaction interface with the 40S ribosome or its zinc-binding motif.
Recent applications extend to studying viral translation strategies, as some pathogens manipulate EIF1 function to hijack host machinery. Additionally, EIF1 overexpression or knockdown models help elucidate its role in cellular stress responses and diseases characterized by translational dysregulation. Despite its small size, EIF1's central regulatory position makes it a valuable tool for both basic research and therapeutic exploration in precision medicine.
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