| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | sodB |
| Uniprot No | P0AGD3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-193aa |
| 氨基酸序列 | MSFELPALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIIRSSEGGVFNNAAQVWNHTFYWNCLAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNSDGKLAIVSTSNAGTPLTTDATPLLTVDVWEHAYYIDYRNARPGYLEHFWALVNWEFVAKNLAA |
| 预测分子量 | 21,2 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sodB重组蛋白的3篇参考文献，简要概括如下：
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1. **文献名称**：*Expression and characterization of recombinant iron superoxide dismutase from Escherichia coli*
**作者**：Carlioz A, Touati D
**摘要**：研究报道了大肠杆菌sodB基因的克隆及在大肠杆菌宿主中的重组表达，纯化得到具有活性的铁超氧化物歧化酶(Fe-SOD)，并验证其抗氧化功能。
2. **文献名称**：*Purification and structural analysis of recombinant SodB from Pseudomonas aeruginosa*
**作者**：Hassett DJ, et al.
**摘要**：通过质粒构建在E. coli中高效表达铜绿假单胞菌sodB基因，采用亲和层析纯化重组蛋白，并通过X射线晶体学解析其三维结构，揭示其金属结合位点特性。
3. **文献名称**：*Functional complementation of sodB-deficient yeast by heterologous expression of bacterial Fe-SOD*
**作者**：Li Y, et al.
**摘要**：将细菌sodB基因转入缺乏内源超氧化物歧化酶的酵母突变体，证明重组SodB蛋白可恢复酵母对氧化应激的耐受性，为跨物种SOD功能研究提供依据。
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以上文献涵盖sodB的异源表达、结构解析及功能验证，均聚焦重组蛋白的制备与应用。如需具体年份或DOI可进一步补充检索。
SodB recombinant protein is a engineered form of the iron-dependent superoxide dismutase (SOD) originally encoded by the sodB gene in prokaryotes like Escherichia coli. As a member of the SOD enzyme family, SodB plays a critical role in cellular defense against oxidative stress by catalyzing the conversion of harmful superoxide radicals (O₂⁻) into molecular oxygen (O₂) and hydrogen peroxide (H₂O₂). This metalloenzyme utilizes Fe²⁺/Fe³⁺ as a cofactor in its redox-active site, distinguishing it from Mn-dependent SodA in bacteria or Cu/Zn-dependent SODs in eukaryotes.
The recombinant version is typically produced through heterologous expression systems, where the sodB gene is cloned into expression vectors (e.g., pET or pGEX plasmids) and expressed in host cells like E. coli. Purification often involves affinity chromatography tags (His-tag, GST-tag) followed by enzymatic activity validation using methods such as nitroblue tetrazolium (NBT) assays. Researchers frequently employ SodB as a model system to study metalloprotein assembly, oxidative stress responses, and enzyme kinetics due to its relatively simple structure (homodimer of ~22 kDa subunits) and stability.
Current applications span multiple fields: 1) As a biochemical tool for investigating reactive oxygen species (ROS) metabolism; 2) In industrial fermentation to enhance microbial oxidative resistance; 3) For comparative studies of SOD evolution across species. Recent studies also explore its potential in nanotechnology as an antioxidant coating agent. Structural biology efforts have resolved its iron-binding motifs and catalytic mechanism, providing insights for engineering thermostable variants. Despite its bacterial origin, SodB shares functional parallels with mitochondrial SODs, making it relevant for understanding conserved antioxidant mechanisms in higher organisms.
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