| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SEPHS1 |
| Uniprot No | P49903 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-392aa |
| 氨基酸序列 | STRESFNPESYELDKSFRLTRFTELKGTGCKVPQDVLQKLLESLQENHFQEDEQFLGAVMPRLGIGMDTCVIPLRHGGLSLVQTTDYIYPIVDDPYMMGRIACANVLSDLYAMGVTECDNMLMLLGVSNKMTDRERDKVMPLIIQGFKDAAEEAGTSVTGGQTVLNPWIVLGGVATTVCQPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVHQWLDIPEKWNKIKLVVTQEDVELAYQEAMMNMARLNRTAAGLMHTFNAHAATDITGFGILGHAQNLAKQQRNEVSFVIHNLPVLAKMAAVSKACGNMFGLMHGTCPETSGGLLICLPREQAARFCAEIKSPKYGEGHQAWIIGIVEKGNRTARIIDKPRIIEVAPQVATQNVNPTPGATS |
| 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. |
以下是关于SEPHS1重组蛋白的3篇代表性文献摘要(注：文献标题及作者为模拟示例，实际文献需通过学术数据库检索确认)：
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1. **标题**：*Expression and Functional Characterization of Recombinant Human SEPHS1 in Cancer Cell Lines*
**作者**：Chen L, et al.
**摘要**：该研究成功在大肠杆菌中表达并纯化了重组人源SEPHS1蛋白，验证其硒磷酸合成酶活性。实验发现，SEPHS1敲低抑制乳腺癌细胞增殖并诱导内质网应激，提示其通过调控硒代谢影响肿瘤生长。
2. **标题**：*Structural Insights into SEPHS1 Catalytic Mechanism via Recombinant Protein Crystallography*
**作者**：Park S, Kim JH
**摘要**：通过重组表达SEPHS1蛋白并进行X射线晶体学分析，揭示了其催化活性位点的三维结构，阐明了其依赖ATP的硒磷酸合成机制，为靶向药物设计提供结构基础。
3. **标题**：*SEPHS1-Mediated Selenium Metabolism Protects Against Oxidative Stress in Mammalian Cells*
**作者**：Müller S, et al.
**摘要**：利用重组SEPHS1蛋白进行体外功能实验，证实其通过合成硒代半胱氨酸前体，增强细胞抗氧化防御能力，在氧化应激条件下维持细胞存活。
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建议通过PubMed或Google Scholar检索关键词“SEPHS1 recombinant protein”获取具体文献。实际研究中，SEPHS1常与癌症代谢、氧化应激及硒蛋白合成通路相关。
SEPHS1 (Selenophosphate Synthetase 1) is a key enzyme involved in selenium metabolism, essential for the biosynthesis of selenoproteins—a unique class of proteins containing the amino acid selenocysteine. Selenoproteins play critical roles in antioxidant defense (e.g., glutathione peroxidases, thioredoxin reductases), thyroid hormone metabolism, and redox signaling. SEPHS1 catalyzes the synthesis of selenophosphate, a selenium donor required for the cotranslational incorporation of selenocysteine into selenoproteins. Unlike its paralog SEPHS2. which is ubiquitously expressed, SEPHS1 exhibits tissue-specific expression and may have distinct regulatory roles in selenium utilization.
Recombinant SEPHS1 protein is generated through molecular cloning and expression in heterologous systems (e.g., E. coli or mammalian cells), enabling researchers to study its enzymatic activity, structure-function relationships, and interactions within the selenoprotein synthesis pathway. Its recombinant form is often tagged for purification and detection, preserving native conformational and catalytic properties. Studies using SEPHS1 recombinant protein have highlighted its potential implications in cancer biology, as dysregulated selenium metabolism is linked to tumor progression and resistance to therapy. SEPHS1 overexpression has been observed in certain cancers, suggesting its role in supporting selenoprotein-dependent survival mechanisms in malignant cells.
Furthermore, SEPHS1 serves as a tool to investigate selenium deficiency disorders and developmental anomalies tied to impaired selenoprotein synthesis. Research on recombinant SEPHS1 also aids in drug discovery, targeting selenium metabolic pathways for therapeutic intervention. Its study contributes to understanding cellular redox homeostasis and the broader interplay between micronutrient metabolism and disease.
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