| WB | 咨询技术 | Human,Mouse,Rat |
| IF | 咨询技术 | Human,Mouse,Rat |
| IHC | 咨询技术 | Human,Mouse,Rat |
| ICC | 技术咨询 | Human,Mouse,Rat |
| FCM | 咨询技术 | Human,Mouse,Rat |
| Elisa | 咨询技术 | Human,Mouse,Rat |
| Aliases | PE1; METS; PE-1; bA110J1.4 |
| Host/Isotype | Rabbit IgG |
| Antibody Type | Primary antibody |
| Storage | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
| Species Reactivity | Human, Mouse |
| Immunogen | Synthetic peptide of human ETV3 |
| Formulation | Purified antibody in PBS with 0.05% sodium azide and 50% glycerol. |
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以下是关于 eIF2B (Phospho-Ser67) 抗体的模拟参考文献示例(仅供参考，建议通过 PubMed 或 Google Scholar 核实真实文献)：
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1. **"Phosphorylation of eIF2Bε on Ser67 modulates translational control in stress responses"**
*Authors: Krishnamoorthy T., Pavitt G.D., et al.*
**摘要**：本研究通过使用 eIF2B (Phospho-Ser67) 特异性抗体，揭示了 eIF2Bε 亚基在丝氨酸 67 位点的磷酸化如何响应内质网应激，进而调控全局蛋白质合成。实验表明，该修饰通过减弱 eIF2B 与 eIF2 的相互作用抑制翻译起始。
2. **"Dynamic regulation of eIF2B phosphorylation by growth factors and nutrient availability"**
*Authors: Wek R.C., Anthony T.G.*
**摘要**：利用 eIF2B (Phospho-Ser67) 抗体的免疫印迹分析，作者发现哺乳动物细胞中雷帕霉素(mTOR)信号通路通过调控 Ser67 磷酸化影响 eIF2B 活性，从而协调细胞增殖与营养状态。
3. **"eIF2B phosphorylation in neurodegenerative disorders: insights from mouse models"**
*Authors: van Kollenburg B., van der Knaap M.S.*
**摘要**：通过免疫组化结合 Phospho-Ser67 抗体，研究报道了脑白质营养不良小鼠模型中 eIF2B 异常磷酸化与髓鞘形成缺陷的相关性，提示磷酸化修饰在神经退行性疾病中的潜在作用。
4. **"A kinase-specific antibody toolkit for dissecting eIF2B regulation"**
*Authors: Hinnebusch A.G., Gómez E.*
**摘要**：本文开发并验证了包括 Phospho-Ser67 在内的一系列 eIF2B 磷酸化抗体，系统分析了不同激酶(如 GSK-3 和 CK2)对 eIF2B 多位点磷酸化的协同调控机制。
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**注意**：上述文献为基于领域知识的模拟示例，实际文献需通过学术数据库检索。建议结合具体研究目标优化关键词(如“eIF2B phosphorylation Ser67”或“antibody validation”)。
The eIF2B (Phospho-Ser67) antibody is designed to detect the phosphorylation of serine residue 67 (Ser67) on the ε-subunit of eukaryotic translation initiation factor 2B (eIF2B), a critical regulator of protein synthesis. eIF2B, a heterodecameric complex (α–ε), acts as a guanine nucleotide exchange factor (GEF) for eIF2. facilitating the recycling of eIF2-GDP to eIF2-GTP during translation initiation. Phosphorylation of eIF2B subunits, including Ser67 on the ε-subunit, modulates its activity in response to cellular stress.
Under stress conditions (e.g., ER stress, nutrient deprivation), kinases such as PERK or GCN2 phosphorylate eIF2α, sequestering eIF2B into inactive complexes and reducing global translation. Phosphorylation of eIF2B itself, including at Ser67. may represent a regulatory feedback mechanism, though its precise role remains under investigation. Some studies suggest that Ser67 phosphorylation could influence eIF2B's GEF activity or interactions with eIF2. impacting translational control during stress adaptation or recovery.
The eIF2B (Phospho-Ser67) antibody is widely used in research to study translational regulation, stress responses, and diseases linked to eIF2B dysfunction, such as vanishing white matter disease (VWMD), where eIF2B mutations impair cellular stress resilience. This antibody is validated for techniques like Western blotting and immunofluorescence, enabling precise detection of phosphorylation dynamics in experimental models. Its application enhances understanding of how post-translational modifications fine-tune protein synthesis in health and disease.
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