| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | XBP1 |
| Uniprot No | P17861 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-185aa |
| 氨基酸序列 | MVVVAAAPNPADGTPKVLLLSGQPASAAGAPAGQALPLMVPAQRGASPEAASGGLPQARKRQRLTHLSPEEKALRRKLKNRVAAQTARDRKKARMSELEQQVVDLEEENQKLLLENQLLREKTHGLVVENQELRQRLGMDALVAEEEAEAKGNEVRPVAGSAESAALRLRAPLQQVQAQLSPLQN |
| 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XBP1重组蛋白的3篇参考文献及其摘要内容：
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1. **文献名称**: *XBP1. a key regulator of unfolded protein response, promotes recombinant protein production in mammalian cells*
**作者**: Lee AH, Iwakoshi NN, Glimcher LH
**摘要**: 该研究探讨了XBP1重组蛋白在哺乳动物细胞中调控未折叠蛋白反应(UPR)的作用。通过过表达剪接型XBP1(XBP1s)，研究者发现其显著增强内质网(ER)的蛋白质折叠能力，并提高重组抗体的分泌效率，为生物制药领域的蛋白生产优化提供了新策略。
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2. **文献名称**: *Engineering recombinant XBP1s to ameliorate ER stress in neurodegenerative disease models*
**作者**: Hetz C, Zhang K, Kaufman RJ
**摘要**: 研究团队通过基因工程构建重组XBP1s蛋白，并在帕金森病细胞模型中验证其功能。结果显示，重组XBP1s能有效激活UPR下游分子伴侣表达，缓解内质网应激导致的神经元损伤，为神经退行性疾病的治疗提供了潜在靶点。
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3. **文献名称**: *Structural and functional analysis of XBP1 splicing mechanism using recombinant protein variants*
**作者**: Yoshida H, Matsui T, Yamamoto A, et al.
**摘要**: 该研究利用重组XBP1蛋白变体(XBP1u和XBP1s)解析其剪接机制。通过体外实验证明，IRE1α激酶介导XBP1u的剪切生成活性形式XBP1s，并揭示其结构域对靶基因启动子结合的调控作用，阐明了UPR信号传导的分子基础。
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这些文献涵盖了XBP1重组蛋白在蛋白质生产、疾病治疗及分子机制中的关键研究，反映了其在基础科学与应用领域的广泛价值。
XBP1 (X-box binding protein 1) is a critical transcription factor central to the unfolded protein response (UPR), a cellular stress mitigation mechanism triggered by endoplasmic reticulum (ER) dysfunction. Discovered in the 1990s, XBP1 exists in two isoforms: the unspliced form (XBP1u) and the spliced active form (XBP1s). Under ER stress, the endoribonuclease IRE1α cleaves XBP1u mRNA, removing a 26-nucleotide intron to produce XBP1s. This spliced variant encodes a functional protein containing a basic leucine zipper (bZIP) domain, enabling it to regulate genes involved in protein folding, ER-associated degradation (ERAD), and lipid biosynthesis.
Recombinant XBP1 protein, typically generated via bacterial or mammalian expression systems, is engineered to mimic the active XBP1s isoform. Its production often involves tagging (e.g., His-tag) for purification and detection. Researchers utilize this recombinant protein to study UPR signaling dynamics, protein-protein interactions, and gene regulation mechanisms in diseases linked to ER stress, including cancer, neurodegenerative disorders (e.g., Alzheimer’s), diabetes, and inflammatory conditions.
In cancer, XBP1s promotes tumor survival under hypoxia and chemotherapy, making it a therapeutic target. In neurodegeneration, its role in resolving protein misfolding has spurred interest in modulating XBP1 activity. Recombinant XBP1 also aids drug discovery, serving as a tool to screen compounds targeting UPR pathways. Despite challenges in maintaining its stability and nuclear localization in experimental models, XBP1 recombinant proteins remain pivotal for dissecting ER stress biology and developing targeted therapies.
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