纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | PSEN2 |
Uniprot No | P49810 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-86 aa |
活性数据 | MLTFMASDSEEEVCDERTSLMSAESPTPRSCQEGRQGPEDGENTAQWRSQENEEDGEEDPDRYVCSGVPGRPPGLEEELTLKYGAK |
分子量 | 35.2 kDa |
蛋白标签 | GST-tag at N-terminal |
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3篇关于重组人PSEN2蛋白的关键文献(示例基于领域内典型研究方向,部分为模拟内容):
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1. **文献名称**: "Expression and Purification of Recombinant Human Presenilin-2 for Structural Studies"
**作者**: Smith A, et al.
**摘要**: 报道了在大肠杆菌中表达并纯化重组人PSEN2蛋白的优化方法,利用His标签和层析技术获得高纯度蛋白,为后续X射线晶体学分析提供材料,并验证其与γ-分泌酶复合体的相互作用能力。
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2. **文献名称**: "Functional Analysis of PSEN2 Mutations in Familial Alzheimer's Disease Using Recombinant Protein Models"
**作者**: Chen L, et al.
**摘要**: 通过重组技术构建PSEN2致病突变体(如N141I),研究其γ-分泌酶活性变化,发现突变导致Aβ42/Aβ40比例升高,提示突变通过改变酶切特异性促进淀粉样斑块形成。
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3. **文献名称**: "Reconstitution of Human γ-Secretase with Recombinant PSEN2 Reveals Subunit-Specific Regulatory Mechanisms"
**作者**: Watanabe H, et al.
**摘要**: 将重组PSEN2与Nicastrin等组分体外组装成功能性γ-分泌酶复合体,证实PSEN2作为催化核心的构象动态性,并揭示APH-1亚基对其稳定性的调控作用。
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4. **文献名称**: "Proteolytic Processing of Recombinant PSEN2 in Mammalian Cells: Implications for Alzheimer's Pathogenesis"
**作者**: Kim Y, et al.
**摘要**: 在哺乳动物细胞中表达重组PSEN2.发现其在内质网中经历自体切割,生成N端和C端片段;抑制切割会降低γ-分泌酶活性,提示自体加工对PSEN2功能的关键性。
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注:以上文献及摘要为示例性质,实际研究中需根据具体需求检索PubMed或Web of Science获取最新论文(可搜索关键词:recombinant PSEN2. γ-secretase, Alzheimer's disease)。
Presenilin-2 (PSEN2) is a multi-pass transmembrane protein encoded by the PSEN2 gene, primarily localized in the endoplasmic reticulum and Golgi apparatus. It is a critical component of the γ-secretase complex, which mediates proteolytic cleavage of type I transmembrane proteins, including amyloid precursor protein (APP). Cleavage of APP by γ-secretase generates amyloid-beta (Aβ) peptides, particularly Aβ40 and Aβ42. Mutations in PSEN2 are linked to early-onset familial Alzheimer's disease (FAD), though less frequently than PSEN1 mutations. These pathogenic variants alter γ-secretase activity, promoting the production of aggregation-prone Aβ42. a hallmark of Alzheimer's pathology.
Recombinant human PSEN2 protein is engineered through heterologous expression systems (e.g., mammalian, insect, or bacterial cells) for structural and functional studies. Its production enables investigation of γ-secretase complex assembly, substrate specificity, and mutation-induced conformational changes. Studies using recombinant PSEN2 have revealed its role in calcium homeostasis, autophagy regulation, and interactions with other AD-associated proteins like nicastrin. Compared to PSEN1. PSEN2 exhibits distinct enzymatic kinetics and substrate preferences, potentially explaining its weaker association with FAD. Current research focuses on developing γ-secretase modulators that selectively target PSEN2 activity to reduce toxic Aβ species while preserving physiological protein processing. However, challenges remain in elucidating PSEN2's full substrate repertoire and non-proteolytic functions in neuronal health.
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