| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ATF6 |
| Uniprot No | P18850 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-202aa |
| 氨基酸序列 | MGEPAGVAGTMESPFSPGLFHRLDEDWDSALFAELGYFTDTDELQLEAAN ETYENNFDNLDFDLDLVPWESDIWDINNQICTVKDIKAEPQPLSPASSSY SVSSPRSVDSYSSTQHVPEELDLSSSSQMSPLSLYGENSNSLSSAEPLKE DKPVTGPRNKTENGLTPKKKIQVNSKPSIQPKPLLLPAAPKTQTISSIPP QT |
| 预测分子量 | 49 kDa |
| 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ATF6重组蛋白的参考文献摘要整理：
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1. **文献名称**: "Activating Transcription Factor 6 (ATF6) Mediates Proteostasis and Longevity in Response to ER Stress"
**作者**: Shoulders, M.D. et al.
**摘要**: 研究揭示了重组ATF6蛋白在细胞应对内质网(ER)应激中的核心作用，通过激活未折叠蛋白反应(UPR)增强蛋白质稳态。实验表明，重组ATF6的活性调控可延长模式生物寿命，提示其潜在治疗应用价值。
2. **文献名称**: "Structural Basis of the Activation of ATF6 by Proteolytic Cleavage during ER Stress"
**作者**: Chen, Y. & Walter, P.
**摘要**: 通过X射线晶体学解析重组ATF6蛋白的活化结构，阐明其在ER应激下被蛋白酶切割的分子机制，揭示其从膜结合前体转化为活性转录因子的构象变化，为靶向药物设计提供依据。
3. **文献名称**: "Recombinant ATF6 Protein Enhances Cellular Resistance to Oxidative Stress via UPR Pathway Activation"
**作者**: Zhang, L. et al.
**摘要**: 利用重组ATF6蛋白处理细胞，发现其通过上调分子伴侣(如BiP)表达缓解氧化应激损伤，证实ATF6重组蛋白在增强细胞适应性反应中的直接作用，提示其在神经退行性疾病中的潜在治疗策略。
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**说明**：以上文献均为示例性整理，实际引用需核对真实出版物信息。建议通过PubMed或Google Scholar以关键词“ATF6 recombinant protein”或“ATF6 activation mechanism”检索最新研究。
ATF6 (Activating Transcription Factor 6) is a key endoplasmic reticulum (ER)-resident sensor protein involved in the unfolded protein response (UPR), a cellular stress mitigation pathway triggered by the accumulation of misfolded proteins in the ER. Structurally, ATF6 contains a luminal stress-sensing domain and a cytoplasmic transcription-activating domain. Under normal conditions, ATF6 remains bound to the ER membrane via its luminal domain and is kept inactive through interactions with ER chaperones like BiP/GRP78. ER stress disrupts these interactions, allowing ATF6 to translocate to the Golgi apparatus, where it undergoes regulated intramembrane proteolysis (RIP). This cleavage releases its cytoplasmic domain, which enters the nucleus to activate transcription of UPR target genes, including those encoding ER chaperones and folding enzymes, to restore proteostasis.
Recombinant ATF6 proteins, typically produced in mammalian or insect expression systems, are engineered versions designed for functional studies or therapeutic exploration. These proteins may include full-length ATF6. cleaved active forms (e.g., ATF6-N), or domain-specific variants. Researchers utilize recombinant ATF6 to dissect its activation mechanism, screen modulators of the UPR pathway, or develop strategies targeting ER stress-related diseases such as neurodegenerative disorders, diabetes, and cancer. Notably, ATF6α (one of two isoforms) has gained attention for its dual role—while acute activation promotes cell survival, chronic activation may drive apoptosis or pathological processes. Recombinant ATF6 tools are vital in understanding this balance and advancing drug discovery for conditions linked to ER dysfunction.
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