| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PENK |
| Uniprot No | P01210 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-97aa |
| 氨基酸序列 | ECSQDC ATCSYRLVRP ADINFLACVM ECEGKLPSLK IWETCKELLQ LSKPELPQDG TSTLRENSKP EESHLLA |
| 预测分子量 | 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PENK重组蛋白的3篇参考文献示例(注：以下文献为虚构示例，仅供格式参考)：
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1. **标题**：*High-yield expression and purification of recombinant human PENK in Escherichia coli for opioid receptor studies*
**作者**：Zhang Y, et al.
**摘要**：本研究利用大肠杆菌表达系统成功制备了重组人源PENK蛋白，通过密码子优化和诱导条件调控提高了表达量，并采用亲和层析纯化获得高纯度蛋白。该蛋白在体外实验中证实可与阿片受体结合，为镇痛机制研究提供了工具。
2. **标题**：*Functional characterization of PENK-derived peptides from recombinant expression in mammalian cells*
**作者**：Wang X, et al.
**摘要**：通过哺乳动物细胞(HEK293)表达重组PENK，研究其酶解后产生的脑啡肽生物活性。实验表明重组蛋白裂解释放的甲硫氨酸脑啡肽在炎症模型中显著抑制疼痛信号传递，验证了其潜在治疗价值。
3. **标题**：*Development of a secretory PENK expression system in Pichia pastoris: implications for large-scale production*
**作者**：Lee S, et al.
**摘要**：构建了毕赤酵母分泌型表达系统生产重组PENK，优化发酵条件后实现克级产量。纯化蛋白经质谱和N端测序验证结构正确性，为工业化生产神经活性肽前体奠定基础。
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如需真实文献，建议在PubMed或Google Scholar中检索关键词：**recombinant proenkephalin**、**PENK expression**、**enkephalin precursor purification**。
PENK (proenkephalin) is a precursor protein encoded by the PENK gene, which plays a critical role in the endogenous opioid system. It serves as the molecular template for enkephalins, small neuropeptides including methionine-enkephalin (Met-Enk) and leucine-enkephalin (Leu-Enk). These peptides function as neurotransmitters and neuromodulators, primarily interacting with δ-opioid and μ-opioid receptors to regulate pain perception, stress responses, and emotional behaviors.
Recombinant PENK protein is artificially produced using genetic engineering techniques, typically through the insertion of the PENK gene into expression vectors (e.g., bacterial, yeast, or mammalian systems). This allows large-scale production of the protein under controlled conditions, ensuring high purity and consistency for research or therapeutic applications. The recombinant form retains the biological activity of natural PENK, enabling precise studies of its processing into active enkephalins and its interactions within neural pathways.
Research on PENK recombinant protein has significant implications for understanding pain mechanisms, addiction, and neurodegenerative disorders. It serves as a tool to investigate enzymatic cleavage processes mediated by proteases like prohormone convertases, which liberate functional enkephalins from the precursor. Additionally, recombinant PENK is explored for potential therapeutic uses, including as a biomarker for cardiovascular and renal diseases, where circulating PENK-derived peptides correlate with disease progression. Its application in drug development focuses on novel analgesics that mimic enkephalins’ effects while avoiding opioid-related side effects. Ongoing studies also examine its role in immune modulation and neuroprotection, highlighting its multifaceted biological relevance.
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