| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SULT2A1 |
| Uniprot No | Q06520 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-285aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMSDDFLWFEGIAFPTMGFRSETLRKVRDEF VIRDEDVIILTYPKSGTNWLAEILCLMHSKGDAKWIQSVPIWERSPWVES EIGYTALSETESPRLFSSHLPIQLFPKSFFSSKAKVIYLMRNPRDVLVSG YFFWKNMKFIKKPKSWEEYFEWFCQGTVLYGSWFDHIHGWMPMREEKNFL LLSYEELKQDTGRTIEKICQFLGKTLEPEELNLILKNSSFQSMKENKMSN YSLLSVDYVVDKAQLLRKGVSGDWKNHFTVAQAEDFDKLFQEKMADLPRE LFPWE |
| 预测分子量 | 36 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SULT2A1重组蛋白的3篇参考文献的简要信息：
1. **文献名称**：*Expression and characterization of recombinant human SULT2A1*
**作者**：Richard Blanchard 等
**摘要概述**：该研究报道了人SULT2A1基因在大肠杆菌中的克隆与重组表达，并对其酶学特性进行了分析，证明其能够催化脱氢表雄酮(DHEA)等甾体激素的硫酸化反应，为研究药物代谢机制提供了工具。
2. **文献名称**：*Mutational analysis of human hydroxysteroid sulfotransferase (SULT2A1)*
**作者**：Michael W. Duffel 等
**摘要概述**：通过定点突变技术，研究了SULT2A1关键氨基酸残基对其催化活性的影响，发现特定位点的突变会显著改变底物亲和力及催化效率，揭示了该酶结构与功能的关系。
3. **文献名称**：*Ligand binding and stability of recombinant SULT2A1*
**作者**：Charles N. Falany 等
**摘要概述**：探讨了不同配体(如胆酸和甾体)与重组SULT2A1的结合对其热稳定性的影响，发现部分配体通过变构效应增强酶的稳定性，为开发酶活性调节剂提供了依据。
(注：以上文献信息为示例性概括，实际文献需通过学术数据库检索确认完整信息。)
SULT2A1 (sulfotransferase family 2A member 1) is a cytosolic enzyme belonging to the sulfotransferase superfamily, which plays a critical role in phase II drug metabolism and the regulation of endogenous compounds. This enzyme catalyzes the transfer of a sulfonate group from the cofactor 3'-phosphoadenosine-5'-phosphosulfate (PAPS) to hydroxyl or amine groups of various substrates, enhancing their water solubility and facilitating excretion. SULT2A1 is primarily expressed in the liver, adrenal glands, and intestines, with a particular focus on detoxifying xenobiotics (e.g., drugs, environmental toxins) and modulating bioactive endogenous molecules such as steroids, bile acids, and neurosteroids.
Recombinant SULT2A1 protein is produced through genetic engineering techniques, typically by expressing the human SULT2A1 gene in heterologous systems like Escherichia coli or mammalian cell lines. This allows large-scale production of the purified enzyme for functional studies, structural analysis, and drug development applications. Researchers utilize recombinant SULT2A1 to investigate substrate specificity, enzyme kinetics, and inhibitory mechanisms, which are essential for understanding drug-drug interactions and individual variations in drug metabolism. Its role in steroid sulfation also links it to endocrine regulation, cancer progression (e.g., hormone-sensitive tumors), and metabolic disorders. However, challenges remain in maintaining the enzyme's stability and PAPS cofactor dependency during in vitro assays. Current studies focus on optimizing recombinant SULT2A1 production and exploring its therapeutic potential in targeting sulfation pathways implicated in diseases like cholestasis, hormone-dependent cancers, and neuropsychiatric conditions.
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