| 纯度 | >90%SDS-PAGE. |
| 种属 | Pig |
| 靶点 | PMAP23 |
| Uniprot No | P49930 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 131-153aa |
| 氨基酸序列 | RIIDLLWRVRRPQKPKFVTVWVR |
| 预测分子量 | 19.0 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PMAP23重组蛋白的示例参考文献(注：以下为模拟生成的示例内容，非真实文献，仅供格式参考)：
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1. **文献名称**：*Expression and Antimicrobial Activity of Recombinant PMAP23 in Escherichia coli*
**作者**：Zhang L. et al.
**摘要**：研究通过大肠杆菌重组表达系统成功获得PMAP23蛋白，并证实其对革兰氏阴性菌(如大肠杆菌)和革兰氏阳性菌(如金黄色葡萄球菌)具有显著抑菌活性，最低抑菌浓度(MIC)低至2 μg/mL。
2. **文献名称**：*Mechanism of PMAP23-Induced Membrane Permeabilization in Bacterial Cells*
**作者**：Wang Y. et al.
**摘要**：通过荧光染料渗漏实验和电镜观察，揭示PMAP23通过破坏细菌细胞膜完整性发挥杀菌作用，其作用机制与阳离子肽的静电相互作用及疏水性结构相关。
3. **文献名称**：*Enhancing the Stability of Recombinant PMAP23 via Site-Directed Mutagenesis*
**作者**：Chen H. et al.
**摘要**：通过定点突变技术改良PMAP23的蛋白酶抗性，获得半衰期延长至天然肽3倍的重组变体，同时保留抗菌活性，为临床应用提供潜在候选分子。
4. **文献名称**：*In Vivo Efficacy of PMAP23 Against Multidrug-Resistant Pseudomonas aeruginosa Infections*
**作者**：Kim S. et al.
**摘要**：在小鼠皮肤感染模型中，局部应用重组PMAP23显著降低耐多药铜绿假单胞菌的细菌载量，并减轻炎症反应，表明其治疗耐药菌感染的潜力。
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**注意**：以上文献为模拟生成内容，实际引用时请通过PubMed、Web of Science等数据库检索真实文献。建议使用关键词“PMAP23 recombinant protein”“antimicrobial peptide PMAP23”进行搜索。
PMAP23 (Porcine Myeloid Antimicrobial Peptide 23) is a cationic host defense peptide derived from the cathelicidin family, originally identified in porcine bone marrow cells. With a length of 23 amino acids, it exhibits a β-hairpin-like structure stabilized by two disulfide bonds, contributing to its stability and functional versatility. As a member of antimicrobial peptides (AMPs), PMAP23 plays a critical role in innate immunity, targeting a broad spectrum of pathogens, including Gram-positive and Gram-negative bacteria, fungi, and enveloped viruses. Its mechanism involves disrupting microbial membranes via electrostatic interactions with negatively charged phospholipids, leading to membrane permeabilization and cell death. Additionally, PMAP23 demonstrates immunomodulatory properties, such as neutralizing bacterial endotoxins and modulating cytokine production.
Recombinant PMAP23 is produced using biotechnological platforms like *E. coli* or yeast expression systems, often fused with solubility-enhancing tags to overcome challenges in peptide folding and toxicity to host cells. Research highlights its potential as a therapeutic candidate, particularly in addressing antibiotic-resistant infections. Studies also explore its synergistic effects with conventional antibiotics and applications in antimicrobial coatings for medical devices. Despite its promise, optimization of production yield, stability in physiological conditions, and mitigation of potential cytotoxicity toward mammalian cells remain active areas of investigation. Overall, PMAP23 exemplifies the translational potential of natural AMPs in combating evolving microbial threats while offering insights into peptide engineering for enhanced clinical utility.
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