| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PNMT |
| Uniprot No | P11086 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-282aa |
| 氨基酸序列 | MSGADRSPNAGAAPDSAPGQAAVASAYQRFEPRAYLRNNYAPPRGDLCNP NGVGPWKLRCLAQTFATGEVSGRTLIDIGSGPTVYQLLSACSHFEDITMT DFLEVNRQELGRWLQEEPGAFNWSMYSQHACLIEGKGECWQDKERQLRAR VKRVLPIDVHQPQPLGAGSPAPLPADALVSAFCLEAVSPDLASFQRALDH ITTLLRPGGHLLLIGALEESWYLAGEARLTVVPVSEEEVREALVRSGYKV RDLRTYIMPAHLQTGVDDVKGVFFAWAQKVGL |
| 预测分子量 | 57 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3-4条关于PNMT(苯乙醇胺-N-甲基转移酶)重组蛋白研究的参考文献概要：
1. **"Cloning and expression of human phenylethanolamine N-methyltransferase (PNMT): cDNA and gene structure"**
*作者：Wong DL, et al.*
**摘要**：该研究首次报道了人类PNMT基因的克隆及其在大肠杆菌中的重组表达，分析了PNMT的基因结构，并验证了重组蛋白的催化活性。
2. **"Crystal structure of recombinant human PNMT complexed with S-adenosyl-L-homocysteine and adrenaline"**
*作者：Martin JL, et al.*
**摘要**：通过X射线晶体学解析了重组人PNMT与底物类似物S-腺苷同型半胱氨酸及肾上腺素的复合物结构，揭示了其催化机制和底物结合位点特征。
3. **"Regulation of recombinant PNMT activity by phosphorylation and substrate availability"**
*作者：Evinger MJ, et al.*
**摘要**：研究探讨了磷酸化修饰对重组PNMT酶活性的调控作用，发现特定激酶介导的磷酸化可增强其在应激状态下的肾上腺素合成能力。
4. **"Functional characterization of recombinant rat PNMT inhibitors for hypertension therapy"**
*作者：Hicks SL, et al.*
**摘要**：在大肠杆菌中表达重组大鼠PNMT蛋白，筛选并评估了多种小分子抑制剂，为开发基于PNMT靶点的高血压治疗药物提供依据。
(注：以上文献为示例性概括，实际引用需根据具体研究内容核实。)
**Background of PNMT Recombinant Protein**
Phenylethanolamine N-methyltransferase (PNMT) is a key enzyme in the catecholamine biosynthesis pathway, primarily responsible for catalyzing the conversion of norepinephrine to epinephrine (adrenaline) by transferring a methyl group from S-adenosyl-L-methionine (SAMe). Expressed predominantly in the adrenal medulla and specific brain regions, PNMT plays a critical role in the stress response, cardiovascular regulation, and energy metabolism. Its activity is tightly regulated by glucocorticoids, emphasizing its connection to the hypothalamic-pituitary-adrenal (HPA) axis.
The recombinant form of PNMT is produced using genetic engineering techniques, often expressed in bacterial (e.g., *E. coli*) or mammalian cell systems to ensure proper folding and post-translational modifications. Purification typically involves affinity chromatography, yielding high-purity protein for research and therapeutic applications. Recombinant PNMT retains enzymatic activity, enabling studies on its structure-function relationships, kinetic mechanisms, and inhibition.
Research leveraging PNMT recombinant protein has advanced understanding of its role in diseases such as hypertension, neuroendocrine tumors, and psychiatric disorders like depression and anxiety. It also serves as a tool for drug discovery, particularly in designing inhibitors to modulate adrenergic signaling. Structural studies, including X-ray crystallography, have elucidated its active site and substrate-binding regions, facilitating targeted therapeutic development.
Overall, PNMT recombinant protein is a vital resource for exploring catecholamine biology, developing diagnostic assays, and innovating treatments for adrenergic dysfunction-related conditions. Its study bridges molecular biology, neuroscience, and clinical medicine, highlighting its multidisciplinary significance.
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