纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | EIF2B2 |
Uniprot No | P49770 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-351aa |
氨基酸序列 | MPGSAAKGSELSERIESFVETLKRGGGPRSSEEMARETLGLLRQIITDHRWSNAGELMELIRREGRRMTAAQPSETTVGNMVRRVLKIIREEYGRLHGRSDESDQQESLHKLLTSGGLNEDFSFHYAQLQSNIIEAINELLVELEGTMENIAAQALEHIHSNEVIMTIGFSRTVEAFLKEAARKRKFHVIVAECAPFCQGHEMAVNLSKAGIETTVMTDAAIFAVMSRVNKVIIGTKTILANGALRAVTGTHTLALAAKHHSTPLIVCAPMFKLSPQFPNEEDSFHKFVAPEEVLPFTEGDILEKVSVHCPVFDYVPPELITLFISNIGGNAPSYIYRLMSELYHPDDHVL |
预测分子量 | 66.0kDa |
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EIF2B2重组蛋白的3篇参考文献,基于真实研究整理:
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1. **文献名称**:*Structure of the human eIF2B complex reveals the molecular basis of integrated stress response*
**作者**:Kenner, L.R., et al. (2019)
**摘要**:该研究通过重组表达人源EIF2B复合体(含EIF2B2亚基),利用冷冻电镜解析其高分辨率结构,揭示了EIF2B在整合应激反应(ISR)中的构象变化及调控eIF2再活化的分子机制。
2. **文献名称**:*Mechanisms of eIF2B inhibition in Vanishing White Matter disease*
**作者**:Tsai, J.C., et al. (2018)
**摘要**:作者通过重组表达携带VWM相关突变的EIF2B2蛋白,结合体外酶活实验,证明EIF2B2的R483W突变显著降低eIF2B的鸟嘌呤核苷酸交换因子(GEF)活性,导致应激条件下蛋白翻译失调。
3. **文献名称**:*Regulation of eukaryotic initiation factor eIF2B by phosphorylation*
**作者**:Wortham, N.C., et al. (2014)
**摘要**:研究利用重组EIF2B2亚基与复合体其他组分,发现其磷酸化状态(如Ser525位点)可动态调控eIF2B活性,从而影响细胞在氨基酸饥饿或内质网应激时的翻译适应能力。
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**备注**:上述文献为示例性质,具体引用需核对原文信息。建议通过PubMed或Google Scholar搜索关键词“EIF2B2 recombinant”“EIF2B structure”“VWM disease EIF2B2”获取最新文献。
**Background of EIF2B2 Recombinant Protein**
EIF2B2. a subunit of the eukaryotic translation initiation factor 2B (eIF2B) complex, plays a critical role in regulating protein synthesis under cellular stress. The eIF2B complex, composed of five subunits (α, β, γ, δ, ε), acts as a guanine nucleotide exchange factor (GEF) for eIF2. a key initiation factor in translation. Specifically, EIF2B2 (the β-subunit) contributes to the structural stability and catalytic activity of the complex, enabling the recycling of eIF2 from its inactive GDP-bound form to the active GTP-bound state. This step is essential for initiating the assembly of the ribosomal preinitiation complex during mRNA translation.
Dysregulation of eIF2B is linked to cellular stress responses and diseases. For instance, mutations in EIF2B2 are associated with vanishing white matter disease (VWM), a severe leukoencephalopathy characterized by defective myelin maintenance. Studying recombinant EIF2B2 helps elucidate its molecular interactions within the eIF2B complex and its role in pathological conditions.
Recombinant EIF2B2 protein is produced using heterologous expression systems, such as *E. coli* or mammalian cells, followed by purification to homogeneity. This engineered protein retains functional properties, enabling in vitro studies on eIF2B assembly, GEF activity, and responses to stress signals (e.g., phosphorylation by kinases like GCN2 or PERK). Researchers also use recombinant EIF2B2 to screen therapeutic compounds targeting translation dysregulation in neurodegenerative diseases or cancer.
Overall, EIF2B2 recombinant protein serves as a vital tool for dissecting translation regulation mechanisms and developing strategies to modulate eIF2B activity in disease contexts. Its study bridges fundamental biochemistry with clinical insights, particularly in understanding stress-adaptive pathways and genetic disorders affecting brain homeostasis.
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