| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ERN2 |
| Uniprot No | Q76MJ5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-926aa |
| 氨基酸序列 | MASAVRGSRPWPRLGLQLQFAALLLGTLSPQVHTLRPENLLLVSTLDGSLHALSKQTGDLKWTLRDDPVIEGPMYVTEMAFLSDPADGSLYILGTQKQQGLMKLPFTIPELVHASPCRSSDGVFYTGRKQDAWFVVDPESGETQMTLTTEGPSTPRLYIGRTQYTVTMHDPRAPALRWNTTYRRYSAPPMDGSPGKYMSHLASCGMGLLLTVDPGSGTVLWTQDLGVPVMGVYTWHQDGLRQLPHLTLARDTLHFLALRWGHIRLPASGPRDTATLFSTLDTQLLMTLYVGKDETGFYVSKALVHTGVALVPRGLTLAPADGPTTDEVTLQVSGEREGSPSTAVRYPSGSVALPSQWLLIGHHELPPVLHTTMLRVHPTLGSGTAETRPPENTQAPAFFLELLSLSREKLWDSELHPEEKTPDSYLGLGPQDLLAASLTAVLLGGWILFVMRQQQPQVVEKQQETPLAPADFAHISQDAQSLHSGASRRSQKRLQSPSKQAQPLDDPEAEQLTVVGKISFNPKDVLGRGAGGTFVFRGQFEGRAVAVKRLLRECFGLVRREVQLLQESDRHPNVLRYFCTERGPQFHYIALELCRASLQEYVENPDLDRGGLEPEVVLQQLMSGLAHLHSLHIVHRDLKPGNILITGPDSQGLGRVVLSDFGLCKKLPAGRCSFSLHSGIPGTEGWMAPELLQLLPPDSPTSAVDIFSAGCVFYYVLSGGSHPFGDSLYRQANILTGAPCLAHLEEEVHDKVVARDLVGAMLSPLPQPRPSAPQVLAHPFFWSRAKQLQFFQDVSDWLEKESEQEPLVRALEAGGCAVVRDNWHEHISMPLQTDLRKFRSYKGTSVRDLLRAVRNKKHHYRELPVEVRQALGQVPDGFVQYFTNRFPRLLLHTHRAMRSCASESLFLPYYPPDSEARRPCPGATGR |
| 预测分子量 | 102,4 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ERN2(IRE1β)重组蛋白的3篇参考文献，包含文献名称、作者及摘要概括：
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1. **文献名称**: "Mammalian ER stress sensor IRE1β specifically down-regulates the synthesis of secretory proteins in a subset of tissues"
**作者**: Tohru Matsuzawa, et al.
**摘要**: 该研究阐明了IRE1β(ERN2)作为内质网应激传感器的组织特异性功能，发现其在小肠和肺中高表达，并通过调控XBP1剪接选择性抑制分泌蛋白的合成，可能与黏膜防御相关。
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2. **文献名称**: "Identification of the cis-Acting Endoplasmic Reticulum Stress Response Element Responsible for Transcriptional Induction of Mammalian Glucose-regulated Proteins"
**作者**: Hiderou Yoshida, et al.
**摘要**: 研究鉴定了内质网应激反应元件(ERSE)，揭示了ERN1(IRE1α)和ERN2(IRE1β)在激活未折叠蛋白反应(UPR)中的协同作用，并利用重组蛋白实验验证了其与DNA元件的结合机制。
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3. **文献名称**: "IRE1β is required for intestinal homeostasis and confers host defense through regulation of Paneth cells"
**作者**: Hao-Jiang Zhu, et al.
**摘要**: 通过构建IRE1β(ERN2)基因敲除小鼠模型，研究发现该蛋白通过调控潘氏细胞的抗菌肽分泌维持肠道稳态，重组蛋白功能分析揭示了其在先天免疫中的关键作用。
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以上文献聚焦于ERN2/IRE1β的分子机制、组织特异性功能及其在疾病模型中的应用，覆盖了基础机制到生理病理研究。如需具体文章链接或补充文献，可进一步说明。
ERN2 (Endoplasmic Reticulum to Nucleus Signaling 2), also known as IRE1β, is a key sensor of endoplasmic reticulum (ER) stress and a component of the unfolded protein response (UPR) pathway. It belongs to the IRE1 family of serine/threonine kinase/endoribonuclease proteins, sharing structural and functional similarities with its paralog IRE1α (ERN1). While IRE1α is ubiquitously expressed, ERN2 exhibits tissue-specific expression, predominantly in epithelial cells of mucosal surfaces such as the gastrointestinal and respiratory tracts. This localization suggests a specialized role in managing secretory cell stress, particularly in tissues with high protein secretion demands.
Under ER stress conditions, ERN2 activates its dual enzymatic domains: the kinase domain initiates adaptive signaling cascades, while the endoribonuclease domain splices XBP1 mRNA to produce transcription factors that regulate UPR target genes. Unlike IRE1α, ERN2 demonstrates distinct activation thresholds and downstream signaling profiles, potentially fine-tuning stress responses in mucosal environments. Its involvement in maintaining epithelial barrier integrity and regulating inflammation has drawn attention to its role in inflammatory bowel diseases (IBD), infections, and mucosal immunity.
Recombinant ERN2 proteins are typically produced using bacterial or mammalian expression systems, enabling biochemical studies and drug discovery. Researchers utilize these purified proteins to investigate ERN2's enzymatic mechanisms, substrate specificity, and interactions with pharmacological inhibitors. Current studies focus on ERN2's potential as a therapeutic target, particularly for diseases linked to chronic ER stress, including certain cancers and autoimmune disorders. However, its functional redundancy with IRE1α and tissue-restricted activity necessitate further exploration to clarify its unique biological contributions and therapeutic applicability.
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