| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SOD1 |
| Uniprot No | P00441 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-154aa |
| 氨基酸序列 | MGHHHHHHHH HHSSGHIEGR HMTYARAAAR QARALE+ATKA VCVLKGDGPV QGIINFEQKE SNGPVKVWGS IKGLTEGLHG FHVHEFGDNT AGCTSAGPHF NPLSRKHGGP KDEERHVGDL GNVTADKDGV ADVSIEDSVI SLSGDHCIIG RTLVVHEKAD DLGKGGNEES TKTGNAGSRL ACGVIGIAQ |
| 预测分子量 | 20 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SOD1重组蛋白的3篇代表性文献示例(注：以下内容为模拟示例，实际文献需通过学术数据库检索)：
---
1. **文献名称**：*Recombinant human SOD1 production and purification from E. coli: A model for ALS-related studies*
**作者**：Smith A, et al.
**摘要**：该研究描述了利用大肠杆菌表达系统高效表达和纯化重组人SOD1蛋白的方法，并验证其酶活性，为后续研究SOD1突变体在肌萎缩侧索硬化症(ALS)中的毒性机制提供基础。
2. **文献名称**：*Structural instability of mutant SOD1 aggregates in familial ALS*
**作者**：Jones B, et al.
**摘要**：通过重组表达ALS相关SOD1突变体(如G93A)，发现突变导致蛋白结构不稳定，易形成淀粉样纤维聚集体，揭示了SOD1错误折叠在神经退行性疾病中的关键作用。
3. **文献名称**：*Antioxidant activity of recombinant SOD1 in oxidative stress models*
**作者**：Chen L, et al.
**摘要**：研究验证了重组SOD1蛋白在细胞氧化应激模型中的保护作用，证明其能有效清除超氧化物自由基，为开发基于SOD1的抗氧化疗法提供依据。
---
如果需要具体文献，建议通过PubMed或Web of Science搜索关键词“recombinant SOD1 protein”或“SOD1 expression ALS”获取最新研究。
Superoxide dismutase 1 (SOD1) is a ubiquitously expressed metalloenzyme critical for cellular antioxidant defense. It catalyzes the conversion of harmful superoxide radicals into molecular oxygen and hydrogen peroxide, thereby mitigating oxidative stress. The native human SOD1 protein is a 32 kDa homodimer, with each subunit containing a copper-zinc catalytic site. While primarily cytosolic, it also localizes to organelles like mitochondria.
The SOD1 gene gained prominence due to its link to amyotrophic lateral sclerosis (ALS). Over 200 mutations in SOD1 are associated with familial ALS (fALS), accounting for ~20% of inherited cases. These mutations destabilize the protein’s structure, promoting toxic aggregation and neuronal degeneration. This connection drove extensive research into SOD1’s biochemistry and pathology.
Recombinant SOD1 production typically involves heterologous expression in E. coli or mammalian systems. The gene is cloned into expression vectors, often fused with tags (e.g., His-tag) for purification via affinity chromatography. Bacterial systems yield high quantities but may require refolding to ensure proper metal ion incorporation and enzymatic activity. Eukaryotic systems better replicate post-translational modifications but are costlier.
Recombinant SOD1 is widely used to study ALS mechanisms, particularly mutant protein misfolding, aggregation kinetics, and oxidative damage. It also serves as a tool for drug screening, enabling the identification of compounds that inhibit aggregation or enhance stability. Additionally, it aids in structural studies (e.g., X-ray crystallography) to map mutation-induced conformational changes.
Challenges persist in replicating native SOD1 behavior, as overexpression systems may alter folding or metal binding. Nevertheless, recombinant SOD1 remains indispensable for dissecting ALS pathophysiology and developing targeted therapies. Ongoing efforts focus on optimizing expression protocols and leveraging engineered variants for therapeutic applications.
×
