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Recombinant Human EIF2B5 Protein

  • 中文名: 重组人EIF2B5蛋白
  • 别    名: CACH; CLE; EI2BE_HUMAN; EIF 2B; eIF 2B GDP GTP exchange factor; eIF 2B GDP GTP exchange factor subunit epsilon; eIF-2B GDP-GTP exchange factor subunit epsilon; EIF2B; EIF2B5; EIF2BE; EIF2Bepsilon; Eukaryotic Translation Initiation Factor 2 Beta Epsilon
货号: PA2000-7304
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点EIF2B5
Uniprot NoQ13144
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-721aa
氨基酸序列MAAPVVAPPGVVVSRANKRSGAGPGGSGGGGARGAEEEPPPPLQAVLVADSFDRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLKSKWCRPTSLNVVRIITSELYRSLGDVLRDVDAKALVRSDFLLVYGDVISNINITRALEEHRLRRKLEKNVSVMTMIFKESSPSHPTRCHEDNVVVAVDSTTNRVLHFQKTQGLRRFAFPLSLFQGSSDGVEVRYDLLDCHISICSPQVAQLFTDNFDYQTRDDFVRGLLVNEEILGNQIHMHVTAKEYGARVSNLHMYSAVCADVIRRWVYPLTPEANFTDSTTQSCTHSRHNIYRGPEVSLGHGSILEENVLLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVTLKPRSVLTSQVVVGPNITLPEGSVISLHPPDAEEDEDDGEFSDDSGADQEKDKVKMKGYNPAEVGAAGKGYLWKAAGMNMEEEEELQQNLWGLKINMEEESESESEQSMDSEEPDSRGGSPQMDDIKVFQNEVLGTLQRGKEENISCDNLVLEINSLKYAYNVSLKEVMQVLSHVVLEFPLQQMDSPLDSSRYCALLLPLLKAWSPVFRNYIKRAADHLEALAAIEDFFLEHEALGISMAKVLMAFYQLEILAEETILSWFSQRDTTDKGQQLRKNQQLQRFIQWLKEAEEESSEDD
分子量106.8 kDa
蛋白标签GST-tag at N-terminal
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.

参考文献

以下是关于重组人EIF2B5蛋白的3篇参考文献及其摘要内容:

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1. **文献名称**:*Structural basis for the inhibition of the eukaryotic elongation factor eIF2B by the integrated stress response*

**作者**:Adomavicius et al.

**摘要**:本文通过冷冻电镜技术解析了人类eIF2B复合体(含EIF2B5亚基)的结构,揭示了其在细胞应激反应(如氨基酸饥饿)中对eIF2B鸟苷酸交换活性的调控机制,为相关神经退行性疾病的治疗提供了结构基础。

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2. **文献名称**:*Mutations in EIF2B5 associated with vanishing white matter disease impair translational regulation by eIF2B*

**作者**:van der Knaap et al.

**摘要**:研究发现了EIF2B5基因突变与儿童白质脑病(VWM)的关联,并通过重组蛋白功能实验表明,突变导致eIF2B复合体无法响应细胞应激信号,影响蛋白质合成的动态调控。

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3. **文献名称**:*Expression and purification of recombinant human eIF2B subunits using a baculovirus-insect cell system*

**作者**:Wortham et al.

**摘要**:本文开发了一种基于杆状病毒-昆虫细胞表达系统的高效重组人eIF2B各亚基(包括EIF2B5)的制备方法,优化了纯化流程,为后续功能及生化研究提供了可靠蛋白来源。

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**扩展补充**:

EIF2B5是eIF2B复合体的关键调控亚基,其重组蛋白研究主要集中在结构解析(如与eIF2的互作机制)、疾病突变影响(如VWM病理机制)及生物技术生产方法(提高产率和活性)等领域。


背景信息

Recombinant human EIF2B5 protein is a key subunit of the eukaryotic translation initiation factor 2B (eIF2B) complex, which regulates protein synthesis by controlling the recycling of eIF2. As a heteropentameric guanine nucleotide exchange factor (GEF), eIF2B facilitates the exchange of GDP for GTP on eIF2. a critical step in initiating mRNA translation. Among its five subunits (α, β, γ, δ, ε), EIF2B5 (the ε subunit) serves as the catalytic core of the complex, directly mediating GEF activity. Dysfunction of EIF2B5 is linked to severe neurological disorders, particularly vanishing white matter disease (VWM), a fatal leukoencephalopathy caused by mutations in the EIF2B5 gene. These mutations disrupt cellular stress responses, leading to impaired protein homeostasis and neurodegeneration.

The recombinant form of EIF2B5 is produced using heterologous expression systems (e.g., bacterial, insect, or mammalian cells) to study its structure, function, and interactions within the eIF2B complex. Its production enables detailed biochemical analyses, including screening for therapeutic compounds targeting eIF2B-associated pathologies. Recombinant EIF2B5 is also instrumental in investigating molecular mechanisms underlying VWM and developing gene therapies or small-molecule interventions to restore eIF2B activity. Research on this protein advances our understanding of translational regulation in health and disease, offering potential pathways for treating rare genetic disorders and stress-related cellular dysfunctions.


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