| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | sodC |
| 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3篇与**sodC重组蛋白**相关的示例参考文献(内容为模拟概括，仅供参考)：
1. **文献名称**：*Cloning, Expression, and Characterization of Recombinant Superoxide Dismutase (SodC) from Escherichia coli*
**作者**：Smith A, et al.
**摘要**：本研究克隆并表达了来自大肠杆菌的sodC基因，通过原核表达系统获得高纯度重组蛋白，并验证其抗氧化酶活性，证实其在清除超氧自由基中的功能。
2. **文献名称**：*Functional Analysis of Recombinant SodC in Bacterial Pathogenesis*
**作者**：Sanchez B, et al.
**摘要**：通过构建sodC缺失突变体并回补重组SodC蛋白，证明该蛋白在沙门氏菌抵抗宿主免疫氧化应激中起关键作用，增强细菌存活能力。
3. **文献名称**：*Optimization of SodC Production in Pichia pastoris for Industrial Applications*
**作者**：Wang C, He Y.
**摘要**：优化毕赤酵母表达系统实现sodC的高效分泌表达，纯化后蛋白在高温和极端pH条件下保持稳定，为工业酶制剂开发提供基础。
4. **文献名称**：*Immunogenicity Evaluation of Recombinant SodC as a Vaccine Candidate*
**作者**：Li X, et al.
**摘要**：将重组SodC蛋白作为疫苗抗原进行小鼠免疫实验，结果显示其可诱导特异性抗体并提高宿主对病原菌感染的防御能力。
**提示**：以上为模拟示例，实际文献需通过PubMed/Google Scholar等平台检索关键词(如“recombinant SodC protein”、“SodC expression”)，并参考近年发表的实验研究。
**Background of SodC Recombinant Protein**
SodC, a bacterial superoxide dismutase (SOD), belongs to the Cu/Zn-SOD family and plays a critical role in neutralizing superoxide radicals (O₂⁻), reactive oxygen species (ROS) generated during aerobic metabolism or host immune responses. Unlike SodA and SodB (Fe/Mn-SODs), SodC is often localized in the periplasm of Gram-negative bacteria, such as *Escherichia coli* and *Salmonella*, where it protects against extracellular oxidative stress. This enzyme catalyzes the dismutation of O₂⁻ into oxygen and hydrogen peroxide, mitigating cellular damage and enhancing bacterial survival under hostile conditions, including within host environments.
The recombinant SodC protein is produced via genetic engineering, typically by cloning the *sodC* gene into expression vectors (e.g., pET systems) and overexpressing it in heterologous hosts like *E. coli*. Purification methods, such as affinity chromatography, yield high-purity SodC for functional and structural studies. Recombinant SodC serves as a model to study bacterial oxidative stress adaptation, enzyme kinetics, and metal cofactor incorporation. Its role in virulence has also drawn attention, as pathogens lacking *sodC* often exhibit reduced infectivity, highlighting its potential as a therapeutic target.
Beyond basic research, recombinant SodC finds applications in biotechnology, including antioxidant additive development and enzymatic ROS-scavenging systems. Studies on its structure-function relationships further contribute to protein engineering efforts aimed at enhancing stability or activity for industrial or medical use. Overall, SodC recombinant protein bridges microbial physiology, enzymology, and applied sciences, offering insights into bacterial resilience and strategies to combat infections.
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