| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PS2 |
| Uniprot No | P04155 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-84aa |
| 氨基酸序列 | EAQTETCTVAPRERQNCGFPGVTPSQCANKGCCFDDTVRGVPWCFYPNTIDVPPEEECEF |
| 预测分子量 | 33.7 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PS2(Presenilin-2)重组蛋白的参考文献示例，内容基于真实研究领域概括，具体文献标题和作者为示例性描述：
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1. **文献名称**: "Expression and Functional Characterization of Recombinant Human Presenilin-2 in a Mammalian Cell System"
**作者**: Smith A, et al.
**摘要**: 研究报道了在HEK293细胞中高效表达并纯化人源PS2重组蛋白的方法，通过体外酶活性实验证实其参与γ-分泌酶复合物对淀粉样前体蛋白(APP)的切割，为阿尔茨海默病分子机制研究提供工具。
2. **文献名称**: "Structural Insights into Presenilin-2 Through Cryo-EM Analysis of the γ-Secretase Complex"
**作者**: Brown K, et al.
**摘要**: 利用冷冻电镜技术解析了包含重组PS2蛋白的γ-分泌酶复合物的三维结构，揭示了PS2在底物识别和催化活性中的关键作用，并探讨了其与家族性阿尔茨海默病突变的相关性。
3. **文献名称**: "Functional Impact of Familial Alzheimer’s Disease Mutations on Recombinant PS2 Protein Activity"
**作者**: Chen L, et al.
**摘要**: 通过表达携带家族性突变(如N141I)的PS2重组蛋白，发现突变体显著增强γ-分泌酶对APP的切割，导致β-淀粉样蛋白(Aβ42)生成增加，提示突变通过改变PS2构象影响致病性。
4. **文献名称**: "Optimized Purification of Recombinant Presenilin-2 for Biochemical and Biophysical Studies"
**作者**: Johnson R, et al.
**摘要**: 开发了一种基于昆虫细胞表达系统的PS2重组蛋白高效纯化方案，结合质谱和圆二色谱验证其稳定性，为后续药物筛选及结构功能研究奠定基础。
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**注**：以上文献标题与作者为示例性内容，实际研究中建议通过数据库(如PubMed、Web of Science)检索具体文献。研究重点多集中于PS2在γ-分泌酶复合物中的功能、结构及与阿尔茨海默病的关联。
PS2 (Presenilin-2) is a multi-pass transmembrane protein encoded by the *PSEN2* gene, located on human chromosome 1. It is a critical component of the γ-secretase enzyme complex, which mediates the proteolytic cleavage of type I transmembrane proteins, including amyloid precursor protein (APP). Cleavage of APP by γ-secretase generates amyloid-β (Aβ) peptides, particularly Aβ42. whose aggregation into plaques is a hallmark of Alzheimer’s disease (AD). Mutations in *PSEN2* are linked to early-onset familial AD, underscoring its role in disease pathology.
Recombinant PS2 proteins are engineered to study its structure-function relationships, enzymatic activity, and interaction with γ-secretase subunits (nicastrin, PEN-2. APH-1). These proteins are typically expressed in heterologous systems like *E. coli*, insect cells, or mammalian cell lines, often fused with tags (e.g., His, FLAG) for purification via affinity chromatography. Challenges in producing functional PS2 include its hydrophobic nature, requiring detergent solubilization, and proper co-expression with other γ-secretase components for enzymatic reconstitution.
Research using recombinant PS2 focuses on elucidating mechanisms of Aβ generation, impacts of AD-associated mutations on γ-secretase processivity, and screening for γ-secretase modulators as potential therapeutics. Additionally, PS2 is implicated in calcium homeostasis and autophagy regulation, expanding its relevance beyond Aβ pathology. The development of recombinant PS2 has enabled *in vitro* assays, structural studies (e.g., cryo-EM), and transgenic models to dissect its physiological and pathological roles. Despite progress, complexities in γ-secretase assembly and substrate specificity warrant further exploration using tailored recombinant systems.
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