| 纯度 | >90%SDS-PAGE. |
| 种属 | Pig |
| 靶点 | PMAP36 |
| Uniprot No | P49931 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 130-166aa |
| 氨基酸序列 | VGRFRRLRKKTRKRLKKIGKVLKWIPPIVGSIPLGCG |
| 预测分子量 | 20.3 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PMAP36重组蛋白的3篇参考文献(内容基于真实研究整理，非实际存在的文献)：
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1. **文献名称**: *"Heterologous expression and functional characterization of recombinant PMAP36 in Escherichia coli"*
**作者**: Zhang Y, Wang L, et al.
**摘要**: 本研究成功在大肠杆菌中表达并纯化了重组PMAP36蛋白，优化了诱导条件以提高可溶性表达。体外抑菌实验表明，重组PMAP36对金黄色葡萄球菌和大肠杆菌均表现出显著抗菌活性，最小抑菌浓度(MIC)分别为4 μg/mL和8 μg/mL。
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2. **文献名称**: *"Structural and antimicrobial analysis of PMAP36 derived from porcine myeloid cells"*
**作者**: Chen H, Li X, et al.
**摘要**: 通过固相合成和重组表达获得PMAP36.并利用圆二色谱分析其α-螺旋结构。研究发现，重组PMAP36通过破坏细菌膜完整性发挥杀菌作用，且在低浓度下即可抑制多重耐药菌株(如耐甲氧西林金黄色葡萄球菌)。
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3. **文献名称**: *"Enhancing the stability and therapeutic potential of PMAP36 via site-directed mutagenesis"*
**作者**: Kim S, Park JH, et al.
**摘要**: 通过定点突变技术改造PMAP36的疏水核心，提高了重组蛋白的蛋白酶抗性和热稳定性。改造后的变体在体外和感染小鼠模型中均展现出更强的长效抗菌效果，为开发新型抗菌药物提供了候选分子。
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注：以上文献信息为模拟生成，实际研究中建议通过PubMed或Web of Science以关键词“PMAP36 recombinant”或“PMAP-36 antimicrobial peptide”检索最新文献。
PMAP36 (Pig Myeloid Antimicrobial Peptide 36) is a cationic host defense peptide belonging to the cathelicidin family, originally identified in pigs. As a member of antimicrobial peptides (AMPs), it plays a critical role in innate immunity by exhibiting broad-spectrum activity against bacteria, fungi, and enveloped viruses. Its primary mechanism involves disrupting microbial membranes through electrostatic interactions between its positively charged residues and negatively charged pathogen surfaces, leading to cell lysis. PMAP36 also demonstrates immunomodulatory functions, such as modulating inflammatory responses and promoting wound healing.
Recombinant PMAP36 is produced using genetic engineering techniques, typically involving codon-optimized gene synthesis, cloning into expression vectors (e.g., pET systems), and purification from bacterial hosts like *E. coli*. The recombinant protein often includes affinity tags (e.g., His-tag) for simplified purification. Structural studies reveal an amphipathic α-helical conformation, enhancing its membrane-targeting capability. Compared to natural peptides, recombinant versions offer scalable production and consistent quality for research and therapeutic development.
Current research focuses on its potential as an alternative to conventional antibiotics, particularly against multidrug-resistant pathogens. Studies highlight its synergistic effects with existing drugs and low propensity for resistance development. However, challenges remain in optimizing its stability, reducing cytotoxicity to mammalian cells, and improving pharmacokinetic profiles. PMAP36’s unique properties position it as a promising candidate for novel antimicrobial agents and immune-enhancing therapies, driving ongoing investigations into clinical applications.
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