| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SULT1C2 |
| Uniprot No | O00338 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-296aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMALTSDLGKQIKLKEVEGTLLQPATVDNWS QIQSFEAKPDDLLICTYPKAGTTWIQEIVDMIEQNGDVEKCQRAIIQHRH PFIEWARPPQPSGVEKAKAMPSPRILKTHLSTQLLPPSFWENNCKFLYVA RNAKDCMVSYYHFQRMNHMLPDPGTWEEYFETFINGKVVWGSWFDHVKGW WEMKDRHQILFLFYEDIKRDPKHEIRKVMQFMGKKVDETVLDKIVQETSF EKMKENPMTNRSTVSKSILDQSISSFMRKGTVGDWKNHFTVAQNERFDEI YRRKMEGTSINFCMEL |
| 预测分子量 | 37 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SULT1C2重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*"Expression and Characterization of Recombinant Human SULT1C2 in Bacterial Systems"*
**作者**：Wang, L., et al.
**摘要**：研究报道了在大肠杆菌中成功表达并纯化重组人SULT1C2蛋白，验证其酶活性，发现其对多种酚类化合物(如多巴胺)具有硫酸化活性，为研究药物代谢机制提供工具。
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2. **文献名称**：*"Substrate Specificity and Structural Analysis of Human SULT1C2 in Xenobiotic Metabolism"*
**作者**：Coughtrie, M.W.H., et al.
**摘要**：通过重组SULT1C2的体外实验，系统分析其底物特异性，发现其对环境毒素(如羟基芳香胺)的代谢作用显著，提示其在解毒过程中的潜在功能。
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3. **文献名称**：*"Functional Characterization of SULT1C2 Isoforms: Implications in Hormone Regulation"*
**作者**：Falany, C.N., et al.
**摘要**：利用重组SULT1C2蛋白研究其与甲状腺激素(T3/T4)的相互作用，揭示该酶可能通过硫酸化调节激素活性，为内分泌疾病研究提供新方向。
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**备注**：上述文献信息为示例，实际文献需通过PubMed或Web of Science检索确认。建议使用关键词“SULT1C2 recombinant”或“SULT1C2 expression”进一步查找近年研究。
**Background of SULT1C2 Recombinant Protein**
SULT1C2 (sulfotransferase family 1C member 2) is a cytosolic enzyme belonging to the sulfotransferase (SULT) superfamily, which plays a critical role in the sulfonation of various endogenous and exogenous compounds. This post-translational modification typically involves transferring a sulfonate group from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to hydroxyl or amine groups on substrates, enhancing their solubility for excretion or modulating their bioactivity. SULT1C2 is primarily expressed in fetal tissues and certain adult organs, with implications in hormone regulation, detoxification, and xenobiotic metabolism.
Structurally, SULT1C2 shares a conserved sulfotransferase domain, characterized by a central β-sheet flanked by α-helices, and a PAPS-binding motif critical for catalytic activity. Its substrate specificity includes phenols, estrogens, and therapeutic drugs, though its physiological roles remain less defined compared to other SULT isoforms. Dysregulation of SULT1C2 has been linked to diseases such as cancer, particularly gastrointestinal and thyroid cancers, where its overexpression may influence tumor progression via altered hormone metabolism.
Recombinant SULT1C2 protein is produced using heterologous expression systems (e.g., *E. coli* or mammalian cells) to enable functional and structural studies. Purified recombinant protein retains enzymatic activity, facilitating research on substrate interactions, inhibitor screening, and mechanistic studies of sulfonation pathways. Its applications span drug development, toxicology, and cancer research, offering insights into metabolic pathways and potential therapeutic targets. Ongoing studies aim to clarify its role in disease and exploit its catalytic properties for biomedical innovations.
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