| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SOD4 |
| Uniprot No | O14618 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-274aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMASDSGNQGTLCTLEFAVQMTCQSCVDAVR KSLQGVAGVQDVEVHLEDQMVLVHTTLPSQEVQALLEGTGRQAVLKGMGS GQLQNLGAAVAILGGPGTVQGVVRFLQLTPERCLIEGTIDGLEPGLHGLH VHQYGDLTNNCNSCGNHFNPDGASHGGPQDSDRHRGDLGNVRADADGRAI FRMEDEQLKVWDVIGRSLIIDEGEDDLGRGGHPLSKITGNSGERLACGII ARSAGLFQNPKQICSCDGLTIWEERGRPIAGKGRKESAQPPAHL |
| 预测分子量 | 31 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SOD4重组蛋白的示例参考文献(注：部分内容为示例性概括，实际文献需通过学术数据库核实)：
1. **标题**：*Heterologous Expression and Antioxidant Activity of Recombinant SOD4 from Aspergillus fumigatus*
**作者**：Smith J, et al. (2018)
**摘要**：研究报道了烟曲霉SOD4在大肠杆菌中的重组表达，纯化后显示高比活性，并验证其清除超氧自由基的能力，提示其在工业抗氧化剂开发中的潜力。
2. **标题**：*Cloning and Stress Response Analysis of Oryza sativa SOD4*
**作者**：Zhang L, et al. (2020)
**摘要**：通过水稻SOD4基因的克隆与重组表达，发现该蛋白在盐胁迫下显著增强植物抗氧化能力，为作物抗逆性研究提供依据。
3. **标题**：*Functional Characterization of Recombinant Caenorhabditis elegans SOD4 in Aging*
**作者**：Brown K, et al. (2019)
**摘要**：利用毕赤酵母系统表达线虫SOD4.证实其延缓氧化损伤的作用，并揭示其通过调控ROS水平影响寿命的机制。
4. **标题**：*Structural and Biochemical Insights into Recombinant Human SOD4-like Protein*
**作者**：Lee S, et al. (2021)
**摘要**：解析了一种人源SOD同源重组蛋白(命名为SOD4)的晶体结构，并证明其通过新型催化机制减轻炎症模型中的氧化应激。
**建议**：实际研究中SOD4的命名可能因物种或研究背景而异，推荐通过PubMed、Web of Science等平台，以关键词“SOD4 recombinant protein”或“SOD4 expression”检索最新文献。
**Background of SOD4 Recombinant Protein**
Superoxide dismutases (SODs) are a class of metalloenzymes critical in mitigating oxidative stress by catalyzing the conversion of harmful superoxide radicals into less reactive oxygen species, such as hydrogen peroxide and molecular oxygen. SOD4. a less characterized member of the SOD family, has recently garnered attention due to its unique structural and functional properties. While SOD1 (cytoplasmic), SOD2 (mitochondrial), and SOD3 (extracellular) are well-studied in mammals, SOD4 is often identified in specific organisms or contexts. For instance, in plants like *Arabidopsis thaliana*, SOD4 refers to an iron-dependent SOD isoform localized in peroxisomes, playing a role in stress responses. In microbial systems, SOD4-like enzymes may contribute to pathogen survival under host-derived oxidative stress.
Recombinant SOD4 production leverages biotechnological platforms, such as *E. coli* or yeast expression systems, to achieve high-yield, purified protein for research or therapeutic applications. Engineering SOD4 as a recombinant protein often focuses on enhancing stability, catalytic efficiency, or tissue-targeting capabilities. Its potential applications span biomedical fields, including anti-aging therapies, inflammatory disease management, and neuroprotection, owing to its antioxidant properties. Industrially, recombinant SOD4 may serve as a preservative in food or cosmetics to combat oxidative spoilage.
Challenges in SOD4 production include maintaining proper metal cofactor integration (e.g., Fe, Mn, or Cu/Zn) and ensuring functional folding, particularly for eukaryotic isoforms requiring post-translational modifications. Ongoing research aims to optimize expression systems and explore SOD4’s mechanistic roles in redox biology, paving the way for novel antioxidant-based interventions.
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