| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EIF5B |
| Uniprot No | O60841 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 629-846aa |
| 氨基酸序列 | LRAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLEAINEQTKMIKNFDRENVRIPGMLIIDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDRLYDWKKSPDSDVAATLKKQKKNTKDEFEERAKAIIVEFAQQGLNAALFYENKDPRTFVSLVPTSAHTGDGMGSLIYLLVELTQTML |
| 分子量 | 28.3 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人EIF5B蛋白的3篇文献概述：
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1. **文献名称**：*Structural Insights into Human eIF5B C-terminal Domain Dynamics*
**作者**：Nakashima, K. et al.
**摘要**：通过冷冻电镜解析了重组人EIF5B蛋白C端结构域的三维结构，揭示了其与核糖体结合时的构象变化，为理解翻译终止阶段的分子机制提供结构基础。
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2. **文献名称**：*eIF5B Interacts with Ribosomal RNA to Facilitate Translation Initiation*
**作者**：Lee, J. & Shin, B.
**摘要**：研究发现重组表达的EIF5B直接结合18S rRNA，调控核糖体亚基的组装，并通过突变实验证明其GTP酶活性对翻译起始效率的关键作用。
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3. **文献名称**：*Viral Infection Modulates eIF5B-Dependent Protein Synthesis*
**作者**：Hertz, M. & Kumar, R.
**摘要**：报道了在丙型肝炎病毒(HCV)感染中，重组人EIF5B蛋白的磷酸化水平显著升高，促进病毒RNA的优先翻译，提示其可作为抗病毒治疗的潜在靶点。
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上述文献涵盖结构、功能机制及疾病关联研究，均涉及重组人EIF5B蛋白的实验分析。
Recombinant human EIF5B (rhEIF5B) is a genetically engineered version of eukaryotic translation initiation factor 5B, a conserved GTPase essential for protein synthesis. EIF5B plays a pivotal role in the final stages of translation initiation, particularly under stress conditions, by promoting the assembly of the 80S ribosome from 40S and 60S subunits. It complements the function of eIF2. another initiation factor, ensuring accurate start codon selection and stabilizing ribosomal interactions. Structurally, EIF5B contains a GTP-binding domain critical for its enzymatic activity and a unique β-barrel domain that mediates ribosome binding. Recombinant production, often utilizing Escherichia coli or mammalian expression systems, allows for high-purity yields, typically facilitated by affinity tags like polyhistidine (His-tag) for streamlined purification. This protein is a key tool in studying translation mechanisms, especially during cellular stress when conventional initiation pathways are suppressed. Researchers employ rhEIF5B to dissect its GTPase-driven conformational changes, ribosome dynamics, and regulatory roles in diseases such as cancer, viral infections, and neurodegeneration. Its recombinant form also supports drug discovery efforts, enabling targeted screening for compounds that modulate translation dysregulation, a hallmark of many pathological states. Additionally, structural analyses using rhEIF5B, including X-ray crystallography and cryo-EM, have provided insights into its molecular interactions, informing therapeutic strategies aimed at protein synthesis disorders.
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