| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SULT1A2 |
| Uniprot No | P50226 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-295aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMELIQDISRPPLEYVKGVPLIKYFAEALGP LQSFQARPDDLLISTYPKSGTTWVSQILDMIYQGGDLEKCHRAPIFMRVP FLEFKVPGIPSGMETLKNTPAPRLLKTHLPLALLPQTLLDQKVKVVYVAR NAKDVAVSYYHFYHMAKVYPHPGTWESFLEKFMAGEVSYGSWYQHVQEWW ELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETVDLMVEHTSFK EMKKNPMTNYTTVRREFMDHSISPFMRKGMAGDWKTTFTVAQNERFDADY AEKMAGCSLSFRSEL |
| 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SULT1A2重组蛋白的3篇参考文献的简要概括：
1. **文献名称**：Expression and Characterization of Recombinant Human SULT1A2 Allozymes
**作者**：Wang et al.
**摘要**：研究在大肠杆菌中表达SULT1A2重组蛋白，分析其在不同基因多态性下的酶活性差异，发现特定突变(如Pro90Leu)显著影响底物代谢能力。
2. **文献名称**：Substrate Specificity of Human SULT1A2: A Systematic Analysis of Xenobiotics
**作者**：Nagar et al.
**摘要**：通过重组表达的SULT1A2蛋白，系统测试其对多种药物和环境化合物的磺化活性，发现其对酚类化合物及部分神经递质具有高催化效率。
3. **文献名称**：Functional Characterization of SULT1A2 in Human Liver and Intestinal Tissues
**作者**：Gamage et al.
**摘要**：利用重组SULT1A2对比其在肝肠组织中的表达差异，揭示该酶在肠道药物代谢中的潜在重要性，并验证其与SULT1A1的底物重叠性。
(注：若需实际文献，建议通过PubMed/Google Scholar检索，部分研究可能以SULT1A1为主要对象，因SULT1A2研究相对较少。)
SULT1A2 (sulfotransferase family 1A member 2) is a cytosolic enzyme belonging to the sulfotransferase (SULT) superfamily, which plays a critical role in phase II metabolism. These enzymes catalyze the transfer of a sulfonate group from 3'-phosphoadenosine-5'-phosphosulfate (PAPS) to hydroxyl or amine groups of endogenous compounds (e.g., hormones, neurotransmitters) and xenobiotics (e.g., drugs, environmental toxins), enhancing their solubility for excretion. SULT1A2 is part of the SULT1A subfamily, which shares structural homology but exhibits distinct substrate preferences and tissue expression patterns compared to its closely related isoform SULT1A1. While SULT1A1 is highly expressed in the liver and intestines, SULT1A2 shows broader tissue distribution, including the liver, brain, and gastrointestinal tract, though at lower overall expression levels.
Recombinant SULT1A2 protein is produced using heterologous expression systems (e.g., E. coli, insect, or mammalian cells) to study its enzymatic activity, substrate specificity, and role in drug metabolism. Its recombinant form enables controlled in vitro experiments, bypassing challenges associated with low native expression and instability in biological samples. Researchers use it to investigate interactions with pharmaceuticals, dietary components, and environmental chemicals, as sulfonation can either detoxify compounds or activate procarcinogens. Polymorphisms in the SULT1A2 gene have been linked to interindividual variability in drug response and disease susceptibility, making this protein a focus in pharmacogenomics and toxicology. However, its functional overlap with SULT1A1 and ambiguous substrate profiling in early studies have led to ongoing debates about its distinct physiological roles, driving the need for further characterization using recombinant protein tools.
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