| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SULT1E1 |
| Uniprot No | P49888 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-294aa |
| 氨基酸序列 | MNSELDYYEK FEEVHGILMY KDFVKYWDNV EAFQARPDDL VIATYPKSGT TWVSEIVYMI YKEGDVEKCK EDVIFNRIPF LECRKENLMN GVKQLDEMNS PRIVKTHLPP ELLPASFWEK DCKIIYLCRN AKDVAVSFYY FFLMVAGHPN PGSFPEFVEK FMQGQVPYGS WYKHVKSWWE KGKSPRVLFL FYEDLKEDIR KEVIKLIHFL ERKPSEELVD RIIHHTSFQE MKNNPSTNYT TLPDEIMNQK LSPFMRKGIT GDWKNHFTVA LNEKFDKHYE QQMKESTLKF RTEI |
| 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SULT1E1重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*"Expression and characterization of recombinant human SULT1E1: role in sulfation of estrogens"*
**作者**：Falany CN, Wheeler J, Oh TS, et al.
**摘要**：研究利用昆虫细胞表达系统成功表达并纯化了人源SULT1E1重组蛋白，证实其对雌激素(如雌二醇)具有高亲和力，并阐明了其在激素代谢中的关键作用。
2. **文献名称**：*"Substrate specificity and inhibition of human sulfotransferase 1E1"*
**作者**：Adjei AA, Gaedigk A, Simon SD, et al.
**摘要**：通过大肠杆菌表达系统制备重组SULT1E1蛋白，系统分析其底物特异性，发现其对多种酚类化合物和药物代谢物具有催化活性，并鉴定出多种选择性抑制剂。
3. **文献名称**：*"Structural insights into the catalytic mechanism of human SULT1E1"*
**作者**：Yoshinari K, Nagata K, Ogino M, et al.
**摘要**：利用重组SULT1E1蛋白的晶体结构解析，揭示了其与辅因子PAPS(3'-磷酸腺苷-5'-磷酰硫酸)及底物的结合模式，阐明了酶催化硫酸基转移的分子机制。
(注：以上文献信息为简化示例，实际引用时需核实具体来源及出版年份。)
SULT1E1 (sulfotransferase family 1E member 1) is a cytosolic enzyme belonging to the sulfotransferase superfamily, which plays a critical role in phase II metabolism by catalyzing the transfer of a sulfonate group from the cofactor 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to hydroxyl or amine groups of endogenous and exogenous compounds. This post-translational modification enhances the water solubility of substrates, facilitating their excretion and regulating their bioactivity. SULT1E1 exhibits high affinity for estrogens, including estradiol and estrone, making it pivotal in modulating hormone signaling, particularly in estrogen-sensitive tissues. Dysregulation of SULT1E1 has been implicated in hormone-dependent cancers, endocrine disorders, and drug metabolism variability.
Recombinant SULT1E1 protein is produced via heterologous expression systems (e.g., E. coli, mammalian cells) to study its structure-function relationships, substrate specificity, and inhibitory mechanisms. Its recombinant form enables large-scale purification and standardized assays, overcoming limitations of low endogenous expression in tissues. Researchers employ techniques like X-ray crystallography and kinetic analyses using recombinant SULT1E1 to elucidate catalytic residues, cofactor binding domains, and substrate interactions.
Pharmaceutically, SULT1E1 is a target for drug design due to its role in metabolizing therapeutic agents and endocrine disruptors. Recombinant protein platforms aid in screening inhibitors or modulators to control estrogenic activity or improve drug efficacy. Additionally, it serves as a tool to investigate sulfation pathways in disease models, such as breast cancer and metabolic syndromes. The availability of active, purified recombinant SULT1E1 accelerates both basic research and translational applications in toxicology, endocrinology, and personalized medicine.
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