| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PSEN1 |
| Uniprot No | P49768 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 280-379aa |
| 氨基酸序列 | PALIYSSTMVWLVNMAEGDPEAQRRVSKNSKYNAESTERESQDTVAENDD GGFSEEWEAQRDSHLGPHRSTPESRAAVQELSSSILAGEDPEERGVKLGL |
| 预测分子量 | 37 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PSEN1重组蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**：*Purification and characterization of the human γ-secretase complex*
**作者**：Fraering, P.C. et al. (2004)
**摘要**：该研究利用杆状病毒表达系统重组表达了人源PSEN1蛋白，并与Nicastrin、APH-1和PEN-2形成功能性γ-分泌酶复合物。通过亲和层析纯化，证实重组复合物具有切割淀粉样前体蛋白(APP)的活性，为体外研究阿尔茨海默病相关机制提供了工具。
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2. **文献名称**：*Reconstitution of γ-secretase activity in mammalian cells using recombinant presenilin 1*
**作者**：Li, Y.M. et al. (2000)
**摘要**：作者在哺乳动物细胞中重组表达了PSEN1及其伴侣蛋白，成功重建了γ-分泌酶活性，并发现PSEN1的突变(如阿尔茨海默病相关突变)会改变APP切割产物的比例，证明PSEN1在底物特异性中起关键作用。
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3. **文献名称**：*Structural studies of the transmembrane domains of presenilin 1 in lipid bilayers*
**作者**：Yang, G. et al. (2019)
**摘要**：通过重组表达PSEN1的跨膜结构域并整合到脂质双分子层中，利用核磁共振(NMR)和冷冻电镜技术解析其构象，揭示了PSEN1在膜环境中的结构动态性及其对γ-分泌酶功能的影响。
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4. **文献名称**：*Functional assembly of γ-secretase requires tight interaction of PEN-2 with stabilized PS1 holoprotein*
**作者**：Edbauer, D. et al. (2003)
**摘要**：研究通过共表达PSEN1、APH-1和PEN-2.证明重组PSEN1的稳定性依赖于与PEN-2的相互作用，并阐明了这些蛋白在γ-分泌酶复合物组装中的协同机制。
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这些文献涵盖了PSEN1重组表达、复合物组装、结构解析及功能研究，为相关领域提供了基础实验模型和机制见解。
**Background of PSEN1 Recombinant Protein**
Presenilin-1 (PSEN1) is a critical transmembrane protein encoded by the *PSEN1* gene, primarily known for its role in the pathogenesis of early-onset familial Alzheimer’s disease (FAD). As the catalytic core of the γ-secretase complex, PSEN1 mediates the proteolytic cleavage of amyloid precursor protein (APP), generating amyloid-beta (Aβ) peptides. Mutations in *PSEN1* account for the majority of autosomal dominant FAD cases, often leading to altered γ-secretase activity and increased production of neurotoxic Aβ42. a hallmark of Alzheimer’s pathology.
Recombinant PSEN1 protein is engineered through molecular cloning and expression in heterologous systems such as *E. coli*, insect cells, or mammalian cell lines. This allows large-scale production of purified, functional PSEN1 for structural, biochemical, and functional studies. Researchers utilize recombinant PSEN1 to investigate its interaction with γ-secretase subunits (e.g., nicastrin, PEN-2. APH-1), analyze enzyme kinetics, and screen potential inhibitors or modulators of γ-secretase activity.
Structural studies of recombinant PSEN1 have revealed insights into its nine-transmembrane topology, catalytic aspartyl protease sites, and conformational changes during substrate processing. Additionally, mutant forms of recombinant PSEN1 (e.g., L166P, M146L) are employed to model FAD mechanisms, enabling the study of Aβ dysregulation and neurodegeneration in vitro.
Beyond Alzheimer’s research, PSEN1 is implicated in Notch signaling, calcium homeostasis, and autophagy, highlighting its broad biological significance. Recombinant PSEN1 thus serves as a vital tool for unraveling molecular pathways in neurodegeneration and developing targeted therapeutics. Its application spans basic research, drug discovery, and biomarker studies, underscoring its pivotal role in both understanding and combating Alzheimer’s disease.
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