| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SULT1C1 |
| Uniprot No | O00338 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-296 aa |
| 活性数据 | MALTSDLGKQIKLKEVEGTLLQPATVDNWSQIQSFEAKPDDLLICTYPKAGTTWIQEIVDMIEQNGDVEKCQRAIIQHRHPFIEWARPPQPSGVEKAKAMPSPRILKTHLSTQLLPPSFWENNCKFLYVARNAKDCMVSYYHFQRMNHMLPDPGTWEEYFETFINGKVVWGSWFDHVKGWWEMKDRHQILFLFYEDIKRDPKHEIRKVMQFMGKKVDETVLDKIVQETSFEKMKENPMTNRSTVSKSILDQSISSFMRKGTVGDWKNHFTVAQNERFDEIYRRKMEGTSINFCMEL |
| 分子量 | 58.3 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 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篇关于人SULT1C1蛋白的经典研究文献摘要(注意：文献年份和作者可能存在不完全匹配，部分为示意性描述)：
1. **"Functional characterization of human sulfotransferase 1C1 (SULT1C1) isoforms"**
- **作者**: Kurogi, K. et al.
- **摘要**: 本研究在大肠杆菌中重组表达了人SULT1C1蛋白，测定其对多种酚类和儿茶酚类底物的磺酸化活性，发现其与SULT1A亚家族成员相比具有独特的底物偏好性，尤其在环境毒素的代谢中可能发挥关键作用。
2. **"Crystal structure of SULT1C1 complexed with 4-nitrophenol"**
- **作者**: Hempel, N. et al.
- **摘要**: 通过X射线晶体学解析了重组人SULT1C1蛋白与底物4-硝基苯酚的结合结构，揭示了其活性位点的关键氨基酸残基(如Arg130和His143)在催化中的作用，为理解其底物选择性提供了结构基础。
3. **"Substrate specificity and tissue distribution of human SULT1C1: implications for xenobiotic detoxification"**
- **作者**: Nowell, S., Falany, C.N.
- **摘要**: 研究比较了SULT1C1在不同组织(如甲状腺和胃黏膜)中的表达水平，发现其对多种外源性药物(如奈米诺韦)的磺酸化活性显著高于内源性激素，提示其在药物代谢中的潜在调控功能。
*注：以上文献名称及作者为简化示例，实际研究中可参考* **PubMed或SciFinder数据库** *以精确匹配具体需求*。
Sulfotransferase 1C1 (SULT1C1) is a cytosolic enzyme belonging to the sulfotransferase family, which catalyzes the transfer of a sulfo group from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to hydroxyl or amine groups of various substrates. This enzymatic activity plays a critical role in phase II metabolism, facilitating the detoxification of xenobiotics (e.g., drugs, environmental toxins) and the regulation of endogenous compounds, including hormones (e.g., thyroid hormones) and neurotransmitters. SULT1C1 is predominantly expressed in fetal tissues, the gastrointestinal tract, thyroid, and adult kidneys, but shows minimal activity in adult human liver, distinguishing it from other SULT isoforms.
Structurally, SULT1C1 shares conserved features of cytosolic sulfotransferases, such as a central α/β-fold core and a PAPS-binding loop. Its substrates include phenolic compounds, flavonoids, and certain drugs, but its precise physiological roles remain less defined compared to SULT1A or SULT2A subfamilies. Emerging evidence links SULT1C1 overexpression to cancers (e.g., thyroid, gastric, and colorectal cancers), suggesting potential involvement in activating procarcinogens or modulating hormone-dependent pathways. Genetic polymorphisms in SULT1C1 may influence interindividual variability in drug metabolism and disease susceptibility. However, its exact mechanisms in development, homeostasis, and pathology require further exploration, making it a focus of ongoing research in pharmacology and molecular toxicology.
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