| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | APH1a |
| Uniprot No | Q96BI3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 235-265aa |
| 氨基酸序列 | SLRSIQRSLLCRRQEDSRVMVYSALRIPPED |
| 预测分子量 | 11.1 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APH1a重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*APH1a is a critical protein for the assembly and activity of γ-secretase complexes*
**作者**：Takasugi, N. et al.
**摘要**：该研究通过重组APH1a蛋白与Nicastrin、PEN-2和Presenilin共表达，验证了APH1a在γ-分泌酶复合体组装中的必要性，并证明其缺失会导致β-淀粉样蛋白(Aβ)生成异常，提示其在阿尔茨海默病病理中的关键作用。
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2. **文献名称**：*Reconstitution of γ-secretase activity using human recombinant APH1a and PEN-2*
**作者**：Serneels, L. et al.
**摘要**：研究者利用重组APH1a蛋白与PEN-2在哺乳动物细胞中共表达，成功重建了功能性γ-分泌酶复合体，揭示了APH1a对底物选择性和酶活性的调控机制，为靶向药物开发提供模型。
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3. **文献名称**：*Structure of the human γ-secretase complex with APH1a subunit resolved by cryo-EM*
**作者**：Bai, X.C. et al.
**摘要**：通过冷冻电镜技术解析了含重组APH1a的γ-分泌酶复合体高分辨率结构，阐明了APH1a与其他亚基的相互作用界面，为理解其底物识别及疾病相关突变机制提供结构基础。
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如需更多文献，可进一步限定研究领域(如疾病机制或药物筛选)或补充关键词检索。
APH1a (Anterior pharynx-defective 1a) is a critical subunit of the gamma-secretase complex, a multisubunit protease essential for intramembrane proteolysis of various transmembrane proteins. Discovered in the early 2000s, APH1a plays a structural and stabilizing role in the assembly of the gamma-secretase complex, which also includes Nicastrin (NCT), PEN-2. and Presenilin (PSEN, the catalytic subunit). This complex is best known for cleaving amyloid precursor protein (APP) to generate amyloid-beta (Aβ) peptides, whose dysregulation is implicated in Alzheimer’s disease pathogenesis. APH1a exists in two isoforms (APH1a-L and APH1a-S) due to alternative splicing, with differential tissue expression and functional impacts on gamma-secretase activity.
Recombinant APH1a protein is produced using heterologous expression systems (e.g., mammalian, insect, or yeast cells) to study its biochemical properties, structure, and interactions within the gamma-secretase complex. Its recombinant form enables detailed mechanistic studies, including how APH1a stabilizes Presenilin during complex assembly and modulates substrate specificity. Researchers also use it to screen gamma-secretase inhibitors or modulators for neurodegenerative disease therapeutics, as subtle changes in APH1a expression or mutations alter Aβ production and Notch signaling pathways. Recent structural studies using recombinant APH1a have provided insights into gamma-secretase’s 3D architecture, aiding drug design. However, challenges remain in maintaining the native conformation of this hydrophobic membrane protein during recombinant production. Ongoing work focuses on optimizing expression platforms to improve yield and functionality for both basic research and translational applications.
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