| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SMS |
| Uniprot No | P52788 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-366aa |
| 氨基酸序列 | AAARHSTLDFMLGAKADGETILKGLQSIFQEQGMAESVHTWQDHGYLATYTNKNGSFANL RIYPHGLVLLDLQSYDGDAQGKEEIDSILNKVEERMKELSQDSTGRVKRLPPIVRGGAID RYWPTADGRLVEYDIDEVVYDEDSPYQNIKILHSKQFGNILILSGDVNLAESDLAYTRAI MGSGKEDYTGKDVLILGGGDGGILCEIVKLKPKMVTMVEIDQMVIDGCKKYMRKTCGDVL DNLKGDCYQVLIEDCIPVLKRYAKEGREFDYVINDLTAVPISTSPEEDSTWEFLRLILDL SMKVLKQDGKYFTQGNCVNLTEALSLYEEQLGRLYCPVEFSKEIVCVPSYLELWVFYTVW KKAKP |
| 预测分子量 | 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SMS(鞘磷脂合成酶)重组蛋白相关的文献示例(注：文献标题与作者为模拟，仅供参考)：
1. **文献名称**：*Expression and Functional Characterization of Recombinant Human Sphingomyelin Synthase 1*
**作者**：Tafesse, F.G. et al.
**摘要**：报道了人源SMS1重组蛋白在哺乳动物细胞中的高效表达与纯化，证实其催化鞘磷脂合成的酶活性，并分析其在内质网膜脂质代谢中的调控机制。
2. **文献名称**：*Crystal Structure of Sphingomyelin Synthase from Saccharomyces cerevisiae*
**作者**：Huitema, K. et al.
**摘要**：通过X射线晶体学解析酵母SMS重组蛋白的三维结构，揭示其底物结合域的关键氨基酸残基，为设计小分子抑制剂提供结构基础。
3. **文献名称**：*Role of Recombinant SMS2 in Apoptosis Regulation*
**作者**：Maruyama, H. et al.
**摘要**：利用昆虫杆状病毒系统表达重组人SMS2蛋白，证明其过表达通过调节神经酰胺/鞘磷脂比例抑制细胞凋亡，提示其在癌症中的潜在作用。
4. **文献名称**：*Development of a High-throughput Assay for SMS Activity Using Recombinant Protein*
**作者**：Liu, J. et al.
**摘要**：构建大肠杆菌表达的重组SMS蛋白，并基于荧光底物建立高通量筛选模型，用于发现调控脂代谢的候选药物分子。
*注：以上文献信息为领域相关方向示例，实际文献需通过PubMed/Web of Science等数据库检索确认。*
**Background of Recombinant SMS Protein**
Recombinant SMS (spermine synthase) protein is produced through recombinant DNA technology, enabling precise study and therapeutic applications of this critical enzyme. SMS catalyzes the conversion of spermidine to spermine, a polyamine essential for cellular processes like DNA stabilization, cell proliferation, and apoptosis regulation. Naturally occurring in humans, SMS is encoded by the *SMS* gene, and its dysfunction is linked to Snyder-Robinson syndrome, a rare genetic disorder characterized by intellectual disability, muscle weakness, and skeletal abnormalities.
Traditional methods of studying SMS relied on isolating the protein from biological tissues, which posed challenges in purity, yield, and scalability. Recombinant technology overcomes these limitations by expressing the *SMS* gene in heterologous systems (e.g., *E. coli*, yeast, or mammalian cells), ensuring high-purity, functional protein production. This approach allows researchers to investigate SMS structure-function relationships, enzymatic mechanisms, and interactions with substrates or inhibitors.
Therapeutic interest in recombinant SMS stems from its role in polyamine metabolism, which is dysregulated in cancers, neurodegenerative diseases, and genetic disorders. Recombinant SMS protein could potentially serve as enzyme replacement therapy for SMS deficiency or as a tool to modulate polyamine levels in disease models. Additionally, it aids in drug discovery, facilitating high-throughput screening for SMS-targeted compounds.
Despite progress, challenges remain in optimizing expression systems for proper post-translational modifications and ensuring stability in therapeutic applications. Ongoing research focuses on engineering SMS variants with enhanced catalytic activity or tailored properties, leveraging advances in protein engineering and synthetic biology. Overall, recombinant SMS protein represents a vital resource for both basic science and translational medicine.
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