| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SUOX |
| Uniprot No | P51687 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 80-545aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSESTHIYTKEEVSSHTSPETGIWVTLGS EVFDVTEFVDLHPGGPSKLMLAAGGPLEPFWALYAVHNQSHVRELLAQYK IGELNPEDKVAPTVETSDPYADDPVRHPALKVNSQRPFNAEPPPELLTEN YITPNPIFFTRNHLPVPNLDPDTYRLHVVGAPGGQSLSLSLDDLHNFPRY EITVTLQCAGNRRSEMTQVKEVKGLEWRTGAISTARWAGARLCDVLAQAG HQLCETEAHVCFEGLDSDPTGTAYGASIPLARAMDPEAEVLLAYEMNGQP LPRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRDYKGFSPS VDWETVDFDSAPSIQELPVQSAITEPRDGETVESGEVTIKGYAWSGGGRA VIRVDVSLDGGLTWQVAKLDGEEQRPRKAWAWRLWQLKAPVPAGQKELNI VCKAVDDGYNVQPDTVAPIWNLRGVLSNAW HRVHVYVSP |
| 预测分子量 | 54 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SUOX(亚硫酸盐氧化酶)重组蛋白的3篇代表性文献摘要概括：
1. **"Expression and Characterization of Recombinant Human Sulfite Oxidase"**
- **作者**: Schwarz G., Mendel R.R.
- **摘要**: 该研究利用大肠杆菌表达系统成功表达了重组人源SUOX蛋白，并优化了纯化流程。通过酶动力学分析，证实其具有与天然酶相似的催化活性，为后续功能研究提供了基础。
2. **"Heterologous Production of Sulfite Oxidase in HEK293 Cells for Functional Studies"**
- **作者**: Johnson J.L., Rajagopalan K.V.
- **摘要**: 在HEK293真核系统中表达重组SUOX，发现其依赖钼辅因子(MoCo)的正确修饰才能发挥活性，揭示了真核表达系统对SUOX翻译后修饰的重要性。
3. **"Crystal Structure of Recombinant Chicken Sulfite Oxidase"**
- **作者**: Kisker C., Schindelin H., Pacheco A.
- **摘要**: 通过X射线晶体学解析了重组鸡源SUOX的三维结构，阐明了其钼活性中心与底物结合的关键区域，为理解催化机制提供了结构基础。
*注：文献标题与作者为示例性概括，实际研究中请根据具体论文数据库(如PubMed)核对详细信息。SUOX重组蛋白的研究多聚焦于表达优化、酶学特性及结构功能分析。*
Sulfite oxidase (SUOX) is a critical mitochondrial enzyme involved in sulfur metabolism, primarily responsible for catalyzing the oxidation of sulfite to sulfate, a vital step in the cysteine and methionine degradation pathways. This molybdenum-containing enzyme also plays a key role in detoxifying exogenous sulfites, which are commonly used as preservatives in food and pharmaceuticals. SUOX deficiency, whether genetic or acquired, is linked to severe neurological impairments, developmental delays, and early mortality in humans, underscoring its physiological importance.
Recombinant SUOX protein is produced using biotechnological platforms, such as bacterial (E. coli), yeast, or mammalian expression systems, to overcome limitations of native protein extraction from tissues. These systems enable large-scale production with high purity and consistency, essential for research and therapeutic applications. The recombinant form retains the enzyme's functional domains, including the molybdenum cofactor (Moco) binding site and the heme domain involved in electron transfer, allowing it to mimic native enzymatic activity.
Research on recombinant SUOX focuses on understanding its structure-function relationships, catalytic mechanisms, and role in sulfite toxicity. It also serves as a tool for developing diagnostic assays for sulfite metabolism disorders and exploring enzyme replacement therapies for SUOX-deficient patients. Challenges remain in stabilizing the Moco moiety during production, as its absence renders the enzyme inactive. Recent advances in cofactor incorporation techniques and protein engineering aim to enhance recombinant SUOX stability and efficacy, potentially broadening its applications in biomedicine and industrial biocatalysis.
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