| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PG |
| Uniprot No | P07585 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-359aa |
| 氨基酸序列 | QQRGLFDFMLEDEASGIGPEVPDDRDFEPSLGPVCPFRCQCHLRVVQCSDLGLDKVPKDLPPDTTLLDLQNNKITEIKDGDFKNLKNLHALILVNNKISKVSPGAFTPLVKLERLYLSKNQLKELPEKMPKTLQELRAHENEITKVRKVTFNGLNQMIVIELGTNPLKSSGIENGAFQGMKKLSYIRIADTNITSIPQGLPPSLTELHLDGNKISRVDAASLKGLNNLAKLGLSFNSISAVDNGSLANTPHLRELHLDNNKLTRVPGGLAEHKYIQVVYLHNNNISVVGSSDFCPPGHNTKKASYSGVSLFSNPVQYWEIQPSTFRCVYVRSAIQLGNYK |
| 预测分子量 | 41.7 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. |
以下是关于重组Protegrin(PG)蛋白的3篇示例参考文献，基于假设PG指抗菌肽Protegrin：
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1. **文献名称**：*"High-level expression and purification of recombinant protegrin-1 in Escherichia coli"*
**作者**：Wang, Y. et al.
**摘要**：研究报道了利用大肠杆菌表达系统高效表达重组Protegrin-1(PG-1)，通过融合硫氧还蛋白标签提高可溶性表达，纯化后蛋白对金黄色葡萄球菌和铜绿假单胞菌表现出强抗菌活性。
2. **文献名称**：*"Engineering recombinant PG-2 with reduced cytotoxicity while maintaining antimicrobial potency"*
**作者**：Garcia, A.E. et al.
**摘要**：通过氨基酸替换策略改造PG-2重组蛋白，降低了其对哺乳动物细胞的毒性，同时保留了对多重耐药菌的抑制能力，为临床转化提供了候选分子。
3. **文献名称**：*"Yeast-derived recombinant Protegrin synergizes with conventional antibiotics against biofilm infections"*
**作者**：Li, X. et al.
**摘要**：在毕赤酵母中成功表达重组PG，证明其可破坏细菌生物膜结构，与抗生素联用显著增强对慢性感染的疗效，为联合疗法提供新思路。
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**注**：以上文献为示例性内容，实际研究中请通过学术数据库(如PubMed、Web of Science)以关键词“recombinant Protegrin”或“PG antimicrobial peptide”检索最新文献。若PG指其他蛋白(如纤溶酶原)，需调整检索策略。
**Background of PG Recombinant Protein**
Protegrins (PGs) are a family of small, cationic antimicrobial peptides (AMPs) initially isolated from porcine leukocytes. They exhibit broad-spectrum activity against bacteria, fungi, viruses, and even some cancer cells. Their potent antimicrobial properties stem from their ability to disrupt microbial membranes via electrostatic interactions and pore formation. Naturally occurring protegrins are short peptides (16–18 amino acids) with a β-hairpin structure stabilized by two disulfide bonds, contributing to their stability in diverse environments.
The growing demand for novel antimicrobial agents, particularly amid rising antibiotic resistance, has driven interest in recombinant PG production. Traditional extraction from natural sources is inefficient and costly, limiting scalability. Recombinant DNA technology enables large-scale, cost-effective synthesis of PG proteins in heterologous expression systems such as *E. coli*, yeast, or mammalian cells. However, challenges persist, including host toxicity due to PG’s membrane-lytic activity, low yield, and the need for post-translational modifications (e.g., disulfide bond formation) to maintain bioactivity.
Recent advancements in expression vector design, fusion tags, and codon optimization have improved PG production. Strategies like inducible promoters, secretion systems, or fusion with solubility-enhancing partners (e.g., SUMO or thioredoxin) mitigate toxicity and enhance yield. Additionally, engineered PG variants with modified charge, hydrophobicity, or reduced cytotoxicity are being explored to expand therapeutic applications.
PG recombinant proteins hold promise for clinical use (wound healing, anti-infectives), agriculture (animal feed additives), and food preservation. Ongoing research focuses on optimizing production platforms, enhancing stability, and evaluating safety profiles to translate these peptides into viable antimicrobial solutions. Their unique mechanism of action, which reduces the likelihood of resistance development, further underscores their potential as next-generation therapeutics.
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