| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Ab1-40 |
| Uniprot No | Q9Y399 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-296aa |
| 氨基酸序列 | MATSSAALPRILGAGARAPSRWLGFLGKATPRPARPSRRTLGSATALMIRESEDSTDFNDKILNEPLKHSDFFNVKELFSVRSLFDARVHLGHKAGCRHRFMEPYIFGSRLDHDIIDLEQTATHLQLALNFTAHMAYRKGIILFISRNRQFSYLIENMARDCGEYAHTRYFRGGMLTNARLLFGPTVRLPDLIIFLHTLNNIFEPHVAVRDAAKMNIPTVGIVDTNCNPCLITYPVPGNDDSPLAVHLYCRLFQTAITRAKEKRQQVEALYRLQGQKEPGDQGPAHPPGADMSHSL |
| 预测分子量 | 33,2 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Aβ1-40重组蛋白的3篇代表性文献(注：Aβ1-40为β-淀粉样蛋白的常见形式，可能与提问中的“Ab1-40”为同一物质)：
1. **文献名称**：*Expression and purification of recombinant Aβ1-40 and Aβ1-42 in E. coli optimized for in vitro studies*
**作者**：Drews A. et al.
**摘要**：该研究优化了Aβ1-40和Aβ1-42在大肠杆菌中的重组表达方法，通过融合标签提高蛋白可溶性，并利用色谱技术纯化获得高纯度蛋白，为体外淀粉样纤维形成研究提供可靠材料。
2. **文献名称**：*Aβ1-40 oligomers induce neuronal apoptosis via modulating mitochondrial membrane permeability*
**作者**：Chen Y. et al.
**摘要**：探讨Aβ1-40寡聚体通过激活线粒体膜通透性转换孔(mPTP)诱发神经元凋亡的机制，发现其可诱导活性氧(ROS)爆发和细胞色素C释放，为阿尔茨海默病致病机理提供依据。
3. **文献名称**：*Real-time monitoring of Aβ1-40 aggregation using a novel fluorescent biosensor*
**作者**：Li X. et al.
**摘要**：开发了一种基于荧光共振能量转移(FRET)的生物传感器，实时追踪重组Aβ1-40从单体到纤维的动态聚集过程，揭示温度与pH对聚集速率的影响。
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**说明**：以上文献为示例性质，实际文献需通过学术数据库(如PubMed、Web of Science)检索。建议结合具体研究方向补充关键词(如“Alzheimer’s disease”“aggregation mechanism”)获取更相关文献。
**Background of Aβ1-40 Recombinant Protein**
Aβ1-40 is a 40-amino acid peptide derived from the proteolytic processing of amyloid precursor protein (APP), a transmembrane protein implicated in Alzheimer’s disease (AD). As one of the predominant amyloid-beta (Aβ) isoforms, Aβ1-40 is generated alongside the more aggregation-prone Aβ1-42 through sequential cleavage by β- and γ-secretases. While Aβ1-42 is strongly linked to AD pathology due to its higher propensity to form neurotoxic oligomers and fibrils, Aβ1-40 constitutes the majority of soluble Aβ species in physiological conditions and exhibits relatively lower aggregation tendencies.
Recombinant Aβ1-40 is artificially produced using expression systems such as *E. coli*, enabling controlled studies of its biophysical and biochemical properties. Unlike native Aβ peptides, recombinant forms lack post-translational modifications, simplifying mechanistic research. Recombinant Aβ1-40 is widely utilized to investigate Aβ aggregation kinetics, structure-function relationships, and interactions with metals, lipids, or therapeutic agents. It also serves as a reference material for developing diagnostic assays or screening anti-amyloid compounds.
Despite its utility, recombinant Aβ1-40 preparations may exhibit batch-dependent variability in solubility and aggregation behavior, requiring rigorous quality control. Studies using recombinant Aβ1-40 have contributed to understanding its role in vascular dysfunction, synaptic toxicity, and inflammation, though its pathophysiological relevance remains debated compared to Aβ1-42. Nonetheless, Aβ1-40 remains a critical tool for modeling early-stage Aβ-mediated mechanisms and validating therapeutic strategies targeting amyloidogenesis in neurodegenerative diseases.
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