| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IAPP |
| Uniprot No | P10997 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 34-70aa |
| 氨基酸序列 | KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY |
| 预测分子量 | 31.4 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IAPP(胰岛淀粉样多肽)重组蛋白研究的参考文献示例(注：文献信息为示例，非真实引用)：
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1. **《Expression and Purification of Recombinant Human Islet Amyloid Polypeptide in E. coli》**
**作者**: S.A. Jayasinghe, R. Langen
**摘要**: 研究通过大肠杆菌表达系统优化重组人IAPP的可溶性表达及纯化策略，用于后续的淀粉样纤维形成机制和结构分析。
2. **《In Vitro Aggregation and Cytotoxicity of Recombinant IAPP in Pancreatic β-Cells》**
**作者**: J. Janson, M.F. Dunn
**摘要**: 探讨重组IAPP在体外形成淀粉样纤维的过程及其对胰岛β细胞的毒性作用，揭示其与2型糖尿病发展的关联。
3. **《Recombinant IAPP as a Model for Amyloidogenesis: Mechanistic Insights》**
**作者**: P. Westermark, K.H. Johnson
**摘要**: 利用重组IAPP蛋白研究淀粉样沉积的动力学和分子机制，评估环境因素(如pH、金属离子)对其聚集的影响。
4. **《Targeting Recombinant IAPP Misfolding for Therapeutic Intervention》**
**作者**: A. Abedini, F. Meng
**摘要**: 分析重组IAPP的错误折叠途径，并筛选小分子抑制剂以阻止其病理性聚集，为糖尿病治疗提供潜在策略。
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**注意**：以上文献标题及内容为模拟示例，具体研究需通过学术数据库(如PubMed、Web of Science)检索核实。实际研究中，重组IAPP的制备常涉及原核/真核表达系统优化，并用于淀粉样蛋白的生化、结构及病理分析。
**Background of Recombinant IAPP Protein**
Islet amyloid polypeptide (IAPP), also known as amylin, is a 37-amino-acid hormone co-secreted with insulin by pancreatic β-cells. It plays roles in glucose metabolism, appetite regulation, and gastric emptying. In type 2 diabetes (T2D) and certain neurodegenerative diseases, IAPP aggregates into cytotoxic amyloid fibrils, contributing to β-cell dysfunction and apoptosis. This amyloidogenic property links IAPP to disease pathogenesis, driving interest in studying its structure, aggregation mechanisms, and therapeutic targeting.
Recombinant IAPP production is critical for such research but faces challenges. Native IAPP’s tendency to aggregate and its toxicity to host cells complicate expression. To overcome this, recombinant IAPP is typically produced using bacterial systems (e.g., *E. coli*) with fusion tags like maltose-binding protein (MBP) or thioredoxin to enhance solubility. These tags are later cleaved, yielding pure, bioactive IAPP. Yeast and mammalian systems are less common due to lower yields or cost inefficiency.
Recombinant IAPP enables *in vitro* studies on fibril formation kinetics, structural dynamics, and interactions with potential inhibitors. It also aids in developing disease models and screening antidiabetic or anti-amyloid drugs. However, maintaining its native conformation remains challenging; improper folding or premature aggregation during purification can compromise experimental outcomes.
Recent advances in protein engineering, such as codon optimization, solubility-enhancing tags, and refined purification protocols, have improved recombinant IAPP yield and stability. Despite progress, replicating its physiological behavior—especially in mimicking human-specific aggregation (rodent IAPP lacks amyloidogenicity)—requires careful validation.
Overall, recombinant IAPP is indispensable for unraveling amyloid-related disease mechanisms and accelerating therapeutic innovations, though technical hurdles in production and handling persist.
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