| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Beta-amyloid 42 |
| Uniprot No | P05067 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-770aa |
| 氨基酸序列 | MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFFYGGCGGNRNNFDTEEYCMAVCGSAMSQSLLKTTQEPLARDPVKLPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQAKNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITALQAVPPRPRHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYERMNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANMISEPRISYGNDALMPSLTETKTTVELLPVNGEFSLDDLQPWHSFGADSVPANTENEVEPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN |
| 预测分子量 | 86kDa |
| 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. |
1. **"Purification and characterization of recombinant beta-amyloid 42 for in vitro aggregation studies"** by Walsh DM et al.
*摘要：该研究描述了大肠杆菌中重组β-淀粉样蛋白42(Aβ42)的高效表达与纯化方法，并分析其在体外形成寡聚体和纤维的动力学，探讨其与阿尔茨海默病病理的相关性。*
2. **"Structural analysis of recombinant beta-amyloid 42 aggregates using solid-state NMR"** by Lührs T et al.
*摘要：通过固态核磁共振技术解析重组Aβ42纤维的高分辨率结构，揭示其β折叠构象及分子间相互作用，为靶向药物设计提供结构基础。*
3. **"Recombinant Aβ42 induces synaptic dysfunction and neurotoxicity in primary neurons"** by Shankar GM et al.
*摘要：研究发现重组Aβ42寡聚体能破坏神经元突触可塑性并引发细胞死亡，提示其在阿尔茨海默病早期认知衰退中的关键作用。*
4. **"Optimizing expression and solubility of recombinant beta-amyloid 42 in E. coli"** by Finder VH et al.
*摘要：通过融合标签和优化表达条件提高Aβ42在大肠杆菌中的可溶性产量，建立适用于大规模病理与药物筛选的稳定制备体系。*
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注：以上文献为示例性质，实际引用时需根据具体研究内容核对真实文献来源及细节。
Beta-amyloid 42 (Aβ42) is a peptide fragment derived from the amyloid precursor protein (APP) through sequential proteolytic cleavage by β- and γ-secretases. It consists of 42 amino acids and is a primary component of amyloid plaques, a hallmark of Alzheimer’s disease (AD). Unlike the shorter Aβ40 isoform, Aβ42 exhibits higher aggregation propensity and neurotoxicity, making it a critical focus in AD research.
Recombinant Aβ42 is artificially produced using expression systems like *E. coli*, enabling controlled study of its biophysical and pathological properties. Researchers often employ plasmid vectors to express the peptide, followed by purification via chromatography and refolding steps to achieve the desired conformation. This synthetic approach ensures reproducibility and scalability, addressing challenges in isolating Aβ42 from biological tissues.
In experimental settings, recombinant Aβ42 is used to model amyloid aggregation kinetics, investigate oligomer formation, and assess toxicity in neuronal cell cultures or transgenic animals. Its propensity to form β-sheet-rich fibrils underpins studies on plaque deposition mechanisms. Additionally, it serves as a tool for screening potential therapeutic agents targeting amyloid aggregation or promoting clearance.
However, handling Aβ42 requires caution due to its instability and tendency to aggregate spontaneously. Batch-to-batch variability in recombinant preparations can influence experimental outcomes, emphasizing the need for rigorous quality control. Despite these challenges, recombinant Aβ42 remains indispensable for unraveling AD pathogenesis and advancing drug development, offering insights into molecular interactions, cellular pathways, and potential biomarkers associated with neurodegeneration.
Current research also explores post-translational modifications (e.g., phosphorylation, oxidation) in recombinant Aβ42 to mimic disease-specific variants, enhancing translational relevance. These efforts aim to bridge gaps between in vitro models and clinical manifestations, fostering targeted therapeutic strategies.
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