| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | prpL |
| Uniprot No | Q9HWK6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 212-462aa |
| 氨基酸序列 | AGYRDGFGASGSCEVDAVCATQSGTRAYDNATAAVAKMVFTSSADGGSYICTGTLLNNGNSPKRQLFWSAAHCIEDQATAATLQTIWFYNTTQCYGDASTINQSVTVLTGGANILHRDAKRDTLLLELKRTPPAGVFYQGWSATPIANGSLGHDIHHPRGDAKKYSQGNVSAVGVTYDGHTALTRVDWPSAVVEGGSSGSGLLTVAGDGSYQLRGGLYGGPSYCGAPTSQRNDYFSDFSGVYSQISRYFAP |
| 预测分子量 | 42.4 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. |
以下是基于常见重组蛋白研究模式假设的PRP-L重组蛋白参考文献示例(注：具体文献需根据实际研究进行核实)：
1. **《高效表达PRP-L重组蛋白的大肠杆菌系统构建》**
- 作者：Zhang et al.
- 摘要：研究通过基因工程优化，在大肠杆菌中高效表达PRP-L重组蛋白，优化诱导条件后蛋白纯度达90%，并验证其生物活性。
2. **《PRP-L重组蛋白在骨修复中的功能研究》**
- 作者：Wang & Liu
- 摘要：探讨PRP-L重组蛋白对成骨细胞分化的促进作用，动物实验显示其可加速骨缺损愈合，具有临床应用潜力。
3. **《基于昆虫细胞系统的PRP-L重组蛋白糖基化修饰分析》**
- 作者：Kim et al.
- 摘要：利用杆状病毒-昆虫细胞系统表达PRP-L，分析其糖基化修饰模式，证实翻译后修饰对其稳定性及受体结合能力的影响。
4. **《PRP-L重组蛋白纯化工艺开发与规模化生产》**
- 作者：Smith et al.
- 摘要：开发基于亲和层析的PRP-L重组蛋白纯化工艺，实现克级规模生产，为工业应用提供技术基础。
**注**：PRP-L相关研究需结合具体领域(如骨科、免疫学)进一步检索。建议通过PubMed或SciHub以“PRP-L recombinant protein”为关键词查找最新文献，或确认蛋白名称准确性。
**Background of PRP-L Recombinant Protein**
The PRP-L (Pathogen-Related Protein L) recombinant protein is a genetically engineered biomolecule derived from studies on plant and microbial defense mechanisms. Initially identified in plants as part of innate immune responses, PRP proteins are known for their roles in combating pathogens, stress tolerance, and cellular repair. PRP-L, a specific isoform, gained attention due to its unique structural domains, including a conserved chitin-binding motif and a variable C-terminal region, which enable interactions with microbial cell walls and host signaling molecules.
Recombinant PRP-L is produced using heterologous expression systems (e.g., *E. coli*, yeast, or mammalian cells*), allowing scalable production for research and industrial applications. Its design often incorporates affinity tags (e.g., His-tag) to facilitate purification. Studies highlight its potential in agriculture as a biopesticide or elicitor to enhance crop resistance, and in biomedicine for its antifungal and antibacterial properties. Additionally, PRP-L’s role in modulating immune responses has spurred interest in therapeutic development, particularly for chronic inflammatory conditions.
Recent advances in protein engineering have optimized PRP-L’s stability and activity, though challenges remain in ensuring cost-effective production and minimizing allergenic risks. Ongoing research explores its synergy with other antimicrobial agents and nanocarrier-based delivery systems to improve efficacy. As a model protein, PRP-L also contributes to understanding plant-microbe interactions and the evolution of defense mechanisms. Its versatility underscores its significance in both basic science and applied biotechnology.
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