| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Ab1-42 |
| Uniprot No | P47914 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-159aa |
| 氨基酸序列 | MAKSKNHTTHNQSRKWHRNGIKKPRSQRYESLKGVDPKFLRNMRFAKKHNKKGLKKMQANNAKAMSARAEAIKALVKPKEVKPKIPKGVSRKLDRLAYIAHPKLGKRARARIAKGLRLCRPKAKAKAKAKDQTKAQAAAPASVPAQAPKRTQAPTKASE |
| 预测分子量 | 17,7 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Aβ1-42重组蛋白的3篇代表性文献及其摘要概括：
1. **"Recombinant production of amyloid-β peptides for structure-functional studies in Alzheimer's disease research"**
- **作者**: K. Murakami et al.
- **摘要**: 研究通过大肠杆菌重组表达系统生产高纯度Aβ1-42.优化了包涵体溶解与层析纯化流程，并验证了重组蛋白的聚集特性与神经细胞毒性，为阿尔茨海默病机制研究提供工具。
2. **"Expression and purification of amyloid-β 1-42 in a Saccharomyces cerevisiae model system"**
- **作者**: S. S. Jayasinghe & R. Kayed
- **摘要**: 利用酵母表达系统生产可溶性Aβ1-42.结合免疫亲和层析纯化，证明重组蛋白形成寡聚体的能力，并揭示其在神经元突触功能障碍中的作用。
3. **"Structural characterization of recombinant Aβ42 fibrils by cryo-electron microscopy"**
- **作者**: M. Schmidt et al.
- **摘要**: 通过重组技术获得均质Aβ1-42.利用冷冻电镜解析其纤维结构，揭示β折叠片层排列模式，为设计抑制淀粉样纤维化的药物提供结构基础。
*注：以上文献为示例性质，实际引用需根据具体研究检索PubMed或Web of Science获取真实文献。*
Amyloid-beta 1-42 (Aβ1-42) is a 42-amino acid peptide derived from the proteolytic cleavage of amyloid precursor protein (APP) by beta- and gamma-secretases. It is a key component of amyloid plaques, the pathological hallmark of Alzheimer’s disease (AD). Aβ1-42 is more aggregation-prone and neurotoxic than its shorter variant, Aβ1-40. due to its hydrophobic C-terminal residues, which promote self-assembly into oligomers, fibrils, and insoluble plaques. These aggregates disrupt neuronal function, trigger inflammation, and contribute to synaptic loss, making Aβ1-42 a central focus in AD research.
Recombinant Aβ1-42 is produced using genetic engineering techniques, often expressed in bacterial systems like *E. coli* or mammalian cell cultures. The recombinant form allows standardized study of its biophysical properties, toxicity mechanisms, and interactions with potential therapeutics. However, producing soluble, monomeric Aβ1-42 is challenging due to its inherent instability and tendency to aggregate prematurely. Researchers employ denaturing conditions, lyophilization, or peptide solubilization protocols to maintain its native conformation for experimental use.
In studies, recombinant Aβ1-42 is used to model AD pathology *in vitro* and *in vivo*, enabling insights into disease pathways, drug screening, and biomarker development. Despite its technical challenges, such as batch-to-batch variability and aggregation artifacts, recombinant Aβ1-42 remains indispensable for investigating therapeutic strategies targeting amyloid toxicity. Its role in AD pathogenesis and its validation in preclinical models continue to drive efforts to understand and mitigate the progression of neurodegenerative diseases.
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