| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ERN1 |
| Uniprot No | O75460 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-977aa |
| 氨基酸序列 | MPARRLLLLLTLLLPGLGIFGSTSTVTLPETLLFVSTLDGSLHAVSKRTGSIKWTLKEDPVLQVPTHVEEPAFLPDPNDGSLYTLGSKNNEGLTKLPFTIPELVQASPCRSSDGILYMGKKQDIWYVIDLLTGEKQQTLSSAFADSLCPSTSLLYLGRTEYTITMYDTKTRELRWNATYFDYAASLPEDDVDYKMSHFVSNGDGLVVTVDSESGDVLWIQNYASPVVAFYVWQREGLRKVMHINVAVETLRYLTFMSGEVGRITKWKYPFPKETEAKSKLTPTLYVGKYSTSLYASPSMVHEGVAVVPRGSTLPLLEGPQTDGVTIGDKGECVITPSTDVKFDPGLKSKNKLNYLRNYWLLIGHHETPLSASTKMLERFPNNLPKHRENVIPADSEKKSFEEVINLVDQTSENAPTTVSRDVEEKPAHAPARPEAPVDSMLKDMATIILSTFLLIGWVAFIITYPLSMHQQQQLQHQQFQKELEKIQLLQQQQQQLPFHPPGDTAQDGELLDTSGPYSESSGTSSPSTSPRASNHSLCSGSSASKAGSSPSLEQDDGDEETSVVIVGKISFCPKDVLGHGAEGTIVYRGMFDNRDVAVKRILPECFSFADREVQLLRESDEHPNVIRYFCTEKDRQFQYIAIELCAATLQEYVEQKDFAHLGLEPITLLQQTTSGLAHLHSLNIVHRDLKPHNILISMPNAHGKIKAMISDFGLCKKLAVGRHSFSRRSGVPGTEGWIAPEMLSEDCKENPTYTVDIFSAGCVFYYVISEGSHPFGKSLQRQANILLGACSLDCLHPEKHEDVIARELIEKMIAMDPQKRPSAKHVLKHPFFWSLEKQLQFFQDVSDRIEKESLDGPIVKQLERGGRAVVKMDWRENITVPLQTDLRKFRTYKGGSVRDLLRAMRNKKHHYRELPAEVRETLGSLPDDFVCYFTSRFPHLLAHTYRAMELCSHERLFQPYYFHEPPEPQPPVTPDAL |
| 预测分子量 | 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ERN1重组蛋白的3篇参考文献示例：
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1. **"IRE1-mediated splicing of XBP1 mRNA in the unfolded protein response"**
*作者：Calfon, M., et al. (2002)*
摘要：研究利用重组IRE1α(ERN1)蛋白证实其在UPR中通过剪切XBP1 mRNA激活下游应激响应，揭示了其核糖核酸内切酶活性机制。
2. **"Crystal structure of the kinase domain of human IRE1 reveals a conserved activation mechanism"**
*作者：Korennykh, A., et al. (2009)*
摘要：通过重组人源IRE1α激酶结构域的晶体结构解析，阐明了其自磷酸化激活过程及二聚化对酶活性的调控。
3. **"Targeting IRE1 with small molecules counteracts progression of atherosclerosis"**
*作者：Tufanli, O., et al. (2017)*
摘要：利用重组IRE1蛋白进行高通量筛选，发现小分子抑制剂可抑制其激酶活性，为动脉粥样硬化治疗提供潜在策略。
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注：以上文献信息为示例，实际引用时需核实原文准确性。
ERN1 (Endoplasmic Reticulum to Nucleus Signaling 1), also known as IRE1α (Inositol-Requiring Enzyme 1α), is a key sensor of endoplasmic reticulum (ER) stress and a central component of the unfolded protein response (UPR). This evolutionarily conserved transmembrane protein plays a critical role in maintaining cellular homeostasis by detecting protein misfolding in the ER lumen and initiating adaptive signaling pathways. Structurally, ERN1 contains an N-terminal ER-luminal stress-sensing domain, a single transmembrane helix, and a C-terminal cytoplasmic region with both kinase and endoribonuclease activities.
Under normal conditions, ERN1 remains inactive through binding to the chaperone BiP/GRP78. During ER stress caused by factors like nutrient deprivation, hypoxia, or protein overload, BiP dissociates to bind misfolded proteins, allowing ERN1 to dimerize and autophosphorylate. Activated ERN1 cleaves XBP1 mRNA through its endoribonuclease activity, generating a spliced variant (XBP1s) that regulates genes involved in protein folding, degradation, and lipid biosynthesis. Additionally, ERN1 can initiate apoptosis through JNK signaling when stress persists unremedied.
Recombinant ERN1 proteins, typically produced in mammalian or insect expression systems, are valuable tools for studying UPR mechanisms. These purified proteins retain enzymatic activities and enable in vitro investigation of ERN1's dual kinase/RNase functions, inhibitor screening, and structural analyses. Researchers utilize ERN1 recombinant proteins to model stress-related pathologies, including neurodegenerative diseases, diabetes, and cancer, where dysregulated UPR contributes to disease progression. Recent drug discovery efforts targeting ERN1's kinase or RNase domains highlight its therapeutic potential in managing ER stress-associated disorders.
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