| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SOD3 |
| Uniprot No | P08294 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-240aa |
| 氨基酸序列 | WTGEDSAEPNSDSAEWIRDMYAKVTEIWQEVMQRRDDDGALHAACQVQPSATLDAAQPRVTGVVLFRQLAPRAKLDAFFALEGFPTEPNSSSRAIHVHQFGDLSQGCESTGPHYNPLAVPHPQHPGDFGNFAVRDGSLWRYRAGLAASLAGPHSIVGRAVVVHAGEDDLGRGGNQASVENGNAGRRLACCVVGVCGPGLWERQAREHSERKKRRRESECKAA |
| 预测分子量 | 28.1kDa |
| 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SOD3重组蛋白的3篇示例参考文献(内容为模拟概括，建议通过学术数据库核实真实文献)：
1. **文献名称**: "Production and characterization of recombinant human extracellular superoxide dismutase (SOD3)"
**作者**: Karlsson K, et al.
**摘要**: 研究报道了通过哺乳动物细胞表达系统高效生产重组人SOD3的方法，验证了其酶活性与天然蛋白一致，并证明其抗氧化作用在炎症模型中可减轻氧化应激损伤。
2. **文献名称**: "Therapeutic potential of SOD3 in pulmonary hypertension: Recombinant protein delivery attenuates vascular remodeling"
**作者**: Kim YM, et al.
**摘要**: 实验表明，通过腺病毒载体递送重组SOD3至肺动脉高压大鼠模型，可显著抑制超氧化物水平，改善血管功能异常和病理重构，提示其作为治疗肺动脉高压的潜在策略。
3. **文献名称**: "Structural insights into the metal-binding properties of recombinant SOD3 and its role in ischemic heart disease"
**作者**: Nguyen TN, et al.
**摘要**: 通过X射线晶体学解析重组SOD3的结构，揭示其铜锌结合域的关键特征，并在心肌缺血再灌注损伤模型中证实其通过清除自由基发挥心脏保护作用。
**注意**：以上文献信息为示例性质，具体研究请以PubMed、Web of Science等数据库检索结果为准。建议结合关键词"recombinant SOD3"、"extracellular superoxide dismutase"、"therapeutic application"进一步筛选近年高质量论文。
**Background of Recombinant SOD3 Protein**
Superoxide dismutase 3 (SOD3), also known as extracellular superoxide dismutase (EC-SOD), is a member of the SOD family, which plays a critical role in mitigating oxidative stress by catalyzing the dismutation of superoxide radicals into hydrogen peroxide and oxygen. Unlike intracellular SOD isoforms (SOD1 and SOD2), SOD3 is a secreted glycoprotein primarily localized in the extracellular matrix (ECM) and body fluids, where it regulates redox homeostasis in tissues exposed to high oxidative stress, such as blood vessels, lungs, and the central nervous system.
The SOD3 protein is encoded by the *SOD3* gene in humans and features a unique structure comprising an N-terminal signal peptide for secretion, a heparin-binding domain for ECM anchoring, and a catalytic domain containing copper and zinc ions. Its activity is tightly regulated by post-translational modifications, including proteolytic processing and glycosylation. Dysregulation of SOD3 has been linked to pathologies such as hypertension, chronic obstructive pulmonary disease (COPD), and neurodegenerative disorders, underscoring its physiological significance.
Recombinant SOD3 is produced using biotechnological platforms (e.g., bacterial, yeast, or mammalian expression systems) to enable large-scale synthesis for research and therapeutic applications. Challenges in production include maintaining proper protein folding, glycosylation, and stability. Recent advances in protein engineering, such as site-specific mutagenesis or fusion tags, aim to enhance its enzymatic activity, bioavailability, and tissue targeting.
Therapeutic interest in recombinant SOD3 centers on its potential to counteract oxidative damage in conditions like ischemia-reperfusion injury, inflammatory diseases, and diabetes. Preclinical studies highlight its ability to reduce inflammation, improve endothelial function, and protect against organ damage. However, clinical translation faces hurdles, including short plasma half-life and immunogenicity, prompting exploration of delivery strategies like PEGylation or nanoparticle encapsulation.
Overall, recombinant SOD3 represents a promising tool for understanding extracellular redox biology and developing antioxidant therapies, with ongoing research focused on optimizing its production and therapeutic efficacy.
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