| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | COMT |
| Uniprot No | P21964 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 27-271aa |
| 氨基酸序列 | RHWGWGLCLIGWNEFILQPIHNLLMGDTKEQRILNHVLQHAEPGNAQSVL EAIDTYCEQKEWAMNVGDKKGKIVDAVIQEHQPSVLLELGAYCGYSAVRM ARLLSPGARLITIEINPDCAAITQRMVDFAGVKDKVTLVVGASQDIIPQL KKKYDVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVICPGA PDFLAHVRGSSCFECTHYQSFLEYREVVDGLEKAIYKGPGSEAGP |
| 预测分子量 | 53 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3篇关于COMT(儿茶酚-O-甲基转移酶)重组蛋白的参考文献示例(内容为模拟虚构，供参考)：
1. **标题**：*Expression and purification of recombinant human soluble catechol-O-methyltransferase from E. coli*
**作者**：Vidgren J., Tilgmann C., Lundström K.
**摘要**：研究报道了人源可溶性COMT基因在大肠杆菌中的高效表达与纯化方法，分析了重组蛋白的酶动力学特性，证实其甲基转移活性与天然蛋白一致。
2. **标题**：*Crystal structure of rat COMT in complex with S-adenosylmethionine and a catechol inhibitor*
**作者**：Lautala P., Ulmanen I., Taskinen J.
**摘要**：通过X射线晶体学解析了大鼠COMT重组蛋白与辅酶S-腺苷甲硫氨酸及抑制剂的复合物结构，揭示了底物结合位点的关键氨基酸残基及其催化机制。
3. **标题**：*Engineering thermostable COMT variants for industrial biocatalysis*
**作者**：Zhang Y., Li H., Wang M.
**摘要**：通过定向进化技术改造COMT重组蛋白的热稳定性，获得在60℃下仍保持活性的突变体，拓展了其在生物催化合成中的应用潜力。
4. **标题**：*Role of Val108Met polymorphism in recombinant COMT activity and inhibitor sensitivity*
**作者**：Lotta T., Taskinen J., Vidgren J.
**摘要**：比较了COMT基因Val108Met多态性对重组蛋白酶活性及抑制剂(如托卡朋)敏感性的影响，为个体化用药提供理论依据。
(注：以上文献信息为示例性虚构，实际文献需通过PubMed或Web of Science等数据库检索。)
**Background of COMT Recombinant Protein**
Catechol-O-methyltransferase (COMT) is a key enzyme involved in the metabolism of catecholamine neurotransmitters and hormones, such as dopamine, epinephrine, and norepinephrine. It catalyzes the transfer of a methyl group from S-adenosylmethionine (SAM) to catechol substrates, regulating their bioactivity and degradation. COMT exists in two isoforms: membrane-bound (MB-COMT) and soluble (S-COMT), derived from the same gene via alternative promoters. Genetic variations in COMT, particularly the Val158Met polymorphism, are linked to differences in enzyme activity and associated with neurological and psychiatric disorders, including Parkinson’s disease, schizophrenia, and anxiety.
Recombinant COMT proteins are engineered versions of the enzyme produced through heterologous expression systems, such as *E. coli*, yeast, or mammalian cells. These systems enable large-scale production of highly pure, functional COMT for research and therapeutic applications. Recombinant COMT retains enzymatic activity and substrate specificity, making it invaluable for studying catecholamine metabolism, drug interactions, and the development of COMT inhibitors (e.g., entacapone, tolcapone) used in Parkinson’s treatment.
Structural studies using recombinant COMT have elucidated its catalytic mechanism, including Mg²⁺-dependent binding of SAM and substrate recognition. Additionally, recombinant proteins facilitate high-throughput screening for novel inhibitors or modulators. Unlike tissue-extracted COMT, recombinant versions offer batch-to-batch consistency, reduced contamination risks, and scalability. They also enable site-directed mutagenesis to explore functional domains or disease-related mutations.
In summary, recombinant COMT proteins are critical tools for advancing neuroscience, pharmacology, and precision medicine, bridging molecular insights with clinical applications in neuropsychiatric and metabolic disorders.
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