| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SULT1A3 |
| Uniprot No | P0DMM9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-295aa |
| 氨基酸序列 | MELIQDTSRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLINTYPKSGTTWVSQILDMIYQGGDLEKCNRAPIYVRVPFLEVNDPGEPSGLETLKDTPPPRLIKSHLPLALLPQTLLDQKVKVVYVARNPKDVAVSYYHFHRMEKAHPEPGTWDSFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETMDFMVQHTSFKEMKKNPMTNYTTVPQELMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL |
| 预测分子量 | 50.2kDa |
| 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 **SULT1A3 重组蛋白** 的简要参考文献示例(文献信息基于领域内常见研究方向，部分内容为模拟概括)：
1. **标题**: "Expression and Characterization of Recombinant Human SULT1A3 in Escherichia coli"
**作者**: Wang J, et al.
**摘要**: 本研究成功在大肠杆菌中表达了重组人源SULT1A3蛋白，优化了纯化条件并验证其酶活性，证明其对儿茶酚胺类物质(如多巴胺)的磺酸化反应具有高效催化能力。
2. **标题**: "Functional Analysis of SULT1A3 Genetic Variants Using Recombinant Protein Assays"
**作者**: Hildebrandt MA, et al.
**摘要**: 通过构建不同单核苷酸多态性(SNP)的SULT1A3重组蛋白，揭示了特定突变(如R213H)显著降低酶活性和底物亲和力，为个体药物代谢差异提供分子机制解释。
3. **标题**: "Structural Insights into Substrate Specificity of SULT1A3 through X-ray Crystallography"
**作者**: Bidwell LM, et al.
**摘要**: 利用X射线晶体学解析了SULT1A3重组蛋白的三维结构，发现其底物结合口袋的电荷分布与儿茶酚类底物选择性高度相关，为设计特异性抑制剂奠定基础。
4. **标题**: "Comparative Study of SULT1A1 and SULT1A3 Recombinant Enzymes in Drug Metabolism"
**作者**: Coughtrie MWH, et al.
**摘要**: 对比两种同工酶(SULT1A1和SULT1A3)重组蛋白的催化特性，发现SULT1A3对单胺类神经递质的磺酸化活性显著高于SULT1A1.提示其在神经递质调控中的独特作用。
*注：以上文献为示例性质，实际引用需以具体数据库(如PubMed)检索结果为准。建议结合关键词“SULT1A3 recombinant expression/kinetics/structure”进一步筛选文献。*
SULT1A3. also known as sulfotransferase 1A3 or catecholamine sulfotransferase, is a cytosolic enzyme belonging to the sulfotransferase (SULT) superfamily. It plays a critical role in phase II drug metabolism by catalyzing the sulfate conjugation of endogenous compounds and xenobiotics, facilitating their excretion. This enzyme is particularly noted for its high substrate specificity toward catecholamines, including dopamine, epinephrine, and norepinephrine, which distinguishes it from other SULT1A isoforms like SULT1A1. SULT1A3 is predominantly expressed in human tissues such as the gastrointestinal tract, platelets, and brain, suggesting roles in neurotransmitter regulation and detoxification pathways.
Recombinant SULT1A3 protein is produced using heterologous expression systems, such as *E. coli*, insect cells, or mammalian cell lines, enabling large-scale purification for functional studies. Its recombinant form retains catalytic activity, allowing researchers to investigate enzyme kinetics, substrate preferences, and inhibition mechanisms. Structural studies reveal conserved sulfotransferase motifs, including the active site binding 3'-phosphoadenosine-5'-phosphosulfate (PAPS), the universal sulfate donor.
Research on recombinant SULT1A3 has clinical relevance due to its involvement in metabolizing neurotransmitters and drugs like levodopa and acetaminophen. Polymorphisms in the *SULT1A3* gene may influence individual responses to medications or susceptibility to diseases, including cancer and neurological disorders. Additionally, this enzyme’s activity in platelets has been linked to cardiovascular health. Recombinant protein tools are vital for screening drug interactions, studying enzyme regulation, and developing targeted therapies. Ongoing studies aim to clarify its role in disease mechanisms and its potential as a biomarker or therapeutic target.
×
