| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ssuE |
| Uniprot No | P80644 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-191aa |
| 氨基酸序列 | MRVITLAGSPRFPSRSSSLLEYAREKLNGLDVEVYHWNLQNFAPEDLLYARFDSPALKTFTEQLQQADGLIVATPVYKAAYSGALKTLLDLLPERALQGKVVLPLATGGTVAHLLAVDYALKPVLSALKAQEILHGVFADDSQVIDYHHRPQFTPNLQTRLDTALETFWQALHRRDVQVPDLLSLRGNAHA |
| 预测分子量 | 26.9 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ssuE重组蛋白的示例参考文献(注：内容为模拟概括，实际文献需通过学术数据库检索)：
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1. **标题**: *Cloning and Functional Characterization of the ssuE Gene in Escherichia coli*
**作者**: Müller, J. et al.
**摘要**: 研究报道了大肠杆菌ssuE基因的克隆与重组表达，证实其编码的蛋白参与磺酸盐代谢途径，并证明重组ssuE具有硫酯酶活性，可将磺基丙酮转化为亚硫酸盐和丙酮酸。
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2. **标题**: *Crystal Structure of SsuE: Insights into Alkanesulfonate Metabolism*
**作者**: Zhang, L. & Ellis, H.R.
**摘要**: 通过X射线晶体学解析了重组ssuE蛋白的三维结构，揭示了其底物结合位点和催化机制，为理解细菌磺酸盐分解的分子基础提供了结构依据。
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3. **标题**: *SsuD and SsuE Synergy in Bacterial Desulfonation Pathways*
**作者**: van der Ploeg, J.R. et al.
**摘要**: 研究探讨了ssuE与ssuD蛋白在磺酸盐代谢中的协同作用，重组蛋白实验表明二者共同参与将烷基磺酸盐转化为亚硫酸盐的关键步骤，强调了其在硫饥饿条件下的生理重要性。
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4. **标题**: *Biotechnological Applications of Recombinant SsuE in Sulfur Recycling*
**作者**: Patel, R.N. et al.
**摘要**: 评估了重组ssuE在生物降解含硫污染物中的潜力，证明其可在体外高效降解环境中的磺酸类化合物，为工业废水处理提供了新策略。
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建议通过PubMed或Web of Science搜索关键词“ssuE recombinant protein”获取真实文献。
**Background of SsuE Recombinant Protein**
The SsuE protein, encoded by the *ssuE* gene, is a bacterial enzyme initially characterized in *Escherichia coli* and other Gram-negative bacteria. It functions as an alkanesulfonate monooxygenase, playing a critical role in sulfur assimilation pathways under sulfate starvation conditions. This enzyme is part of the SsuDADEF system, which enables bacteria to utilize alternative sulfur sources, such as aliphatic sulfonates, by cleaving the stable C-S bond in these compounds. This process releases sulfite, which is subsequently incorporated into key biomolecules like cysteine and glutathione, essential for cellular metabolism and oxidative stress defense.
SsuE belongs to the flavin reductase family and works in tandem with SsuD, a FMNH₂-dependent monooxygenase. SsuE catalyzes the reduction of flavin adenine dinucleotide (FAD) to FADH₂ using NADH or NADPH as electron donors, providing the necessary cofactor for SsuD’s activity. This partnership highlights its role in a two-component enzymatic system critical for bacterial survival in sulfur-limited environments.
Recombinant SsuE protein is produced via heterologous expression, often in *E. coli* systems, enabling large-scale purification and functional studies. Its recombinant form has been instrumental in elucidating the structural and mechanistic basis of flavin reduction and sulfur scavenging. Studies on SsuE also contribute to understanding bacterial adaptation strategies, potential antimicrobial targets, and applications in bioremediation, where sulfur compound metabolism is relevant. Additionally, insights into SsuE’s role in pathogenicity (e.g., in *Pseudomonas aeruginosa*) underscore its biomedical significance, linking sulfur metabolism to bacterial virulence and host infection processes.
Overall, SsuE recombinant protein serves as a valuable tool for both basic research and applied microbiological studies.
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