| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AOPP |
| Uniprot No | P30044 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 53-214aa |
| 氨基酸序列 | MAPIKVGD AIPAVEVFEG EPGNKVNLAE LFKGKKGVLF GVPGAFTPGC SKTHLPGFVE QAEALKAKGV QVVACLSVND AFVTGEWGRA HKAEGKVRLL ADPTGAFGKE TDLLLDDSLV SIFGNRRLKR FSMVVQDGIV KALNVEPDGT GLTCSLAPNI ISQL |
| 预测分子量 | 22 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AOPP(晚期氧化蛋白产物)重组蛋白研究的3篇参考文献的示例，基于常见研究方向整理而成：
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1. **文献名称**：*Recombinant expression and oxidative modification of human serum albumin: A model for advanced oxidation protein products (AOPP) in vitro*
**作者**：Zhang L, et al.
**摘要**：本研究通过重组技术表达人血清白蛋白(HSA)，并在体外利用次氯酸诱导氧化生成AOPP，分析其结构变化及对巨噬细胞炎症因子(如TNF-α、IL-6)的激活作用，揭示了AOPP在慢性炎症疾病中的潜在机制。
2. **文献名称**：*AOPP-modified recombinant apolipoprotein A-I impairs cholesterol efflux through CD36 pathway*
**作者**：Wang Y, et al.
**摘要**：通过氧化重组载脂蛋白A-I(apoA-I)生成AOPP，发现其抑制巨噬细胞胆固醇外流能力，并证实该过程通过CD36受体介导的脂质蓄积通路，为动脉粥样硬化发病机制提供了新见解。
3. **文献名称**：*Development of a recombinant AOPP detection kit for clinical assessment in renal failure patients*
**作者**：Kim S, et al.
**摘要**：研究开发了一种基于重组β2-微球蛋白氧化产物的AOPP检测试剂盒，验证了其在肾功能衰竭患者血浆中的灵敏度和特异性，证实AOPP水平与疾病严重程度呈正相关，为临床诊断提供了新工具。
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**备注**：以上文献为示例性内容，实际研究中请通过PubMed、Web of Science等数据库检索具体文献(关键词：AOPP/recombinant protein/oxidative stress)。若需开放获取论文，可尝试在*PLOS ONE*或*Scientific Reports*等期刊中查找相关主题。
**Background of AOPP Recombinant Proteins**
AOPP (Advanced Oxidation Protein Product) recombinant proteins are engineered biomolecules designed to mimic or counteract oxidative stress-related modifications in proteins. Oxidative stress, a hallmark of various pathological conditions (e.g., chronic inflammation, neurodegenerative diseases, and diabetes), leads to the formation of AOPPs through chlorinated oxidant reactions, particularly involving myeloperoxidase (MPO) in vivo. These modified proteins serve as biomarkers for oxidative damage and are implicated in disease progression by promoting inflammation and cellular dysfunction.
Recombinant protein technology enables the production of AOPP-modified proteins in controlled laboratory settings. By introducing specific oxidative modifications (e.g., chlorination of tyrosine residues) into recombinant proteins, researchers can systematically study their structural, functional, and immunological properties. This approach aids in elucidating mechanisms of AOPP-induced pathogenesis, such as receptor-mediated signaling (e.g., interaction with RAGE or scavenger receptors) or immune system activation.
Applications of AOPP recombinant proteins span diagnostic, therapeutic, and basic research. They are used to develop assays for quantifying oxidative stress in clinical samples, screen potential antioxidants, and validate therapeutic targets. Additionally, engineered AOPP proteins help in designing decoy molecules or antibodies to neutralize their harmful effects in vivo.
Current challenges include optimizing modification fidelity, scalability, and ensuring biological relevance to native AOPPs. Advances in protein engineering, such as site-specific oxidation and CRISPR-based expression systems, continue to refine their utility in understanding and mitigating oxidative stress-related diseases.
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