| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | PR-10 |
| Uniprot No | P26987 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-158aa |
| 氨基酸序列 | MGVFTFEDEINSPVAPATLYKALVTDADNVIPKALDSFKSVENVEGNGGPGTIKKITFLEDGETKFVLHKIESIDEANLGYSYSVVGGAALPDTAEKITFDSKLVAGPNGGSAGKLTVKYETKGDAEPNQDELKTGKAKADALFKAIEAYLLAHPDYN |
| 预测分子量 | 18.8 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. |
1. **《Structural and immunological characterization of recombinant PR-10 protein from Betula verrucosa》**
- 作者：Breiteneder H. et al.
- 摘要：研究通过大肠杆菌重组表达了桦树花粉中的PR-10蛋白(Bet v 1)，分析了其三维结构及与IgE抗体的结合能力，揭示了其作为主要过敏原的分子基础。
2. **《Recombinant PR-10 allergens in the diagnosis of pollen-related food allergy》**
- 作者：Vieths S., Scheurer S.
- 摘要：探讨重组PR-10蛋白(如Mal d 1苹果过敏原)在交叉反应性食物过敏诊断中的应用，证明其可提高临床检测特异性，减少误诊。
3. **《Expression and epitope mapping of PR-10 family proteins for immunotherapy development》**
- 作者：Ferreira F. et al.
- 摘要：利用重组PR-10蛋白筛选T细胞和B细胞表位，评估其作为变应原特异性免疫治疗疫苗的潜力，发现关键表位可降低过敏反应。
4. **《Comparative study of native and recombinant PR-10 allergen stability》**
- 作者：Radauer C. et al.
- 摘要：对比天然与重组PR-10蛋白的热稳定性和酶解敏感性，发现重组蛋白在保留免疫原性的同时更易标准化生产，适用于临床试剂开发。
PR-10 (Pathogenesis-Related 10) proteins are a conserved family of small, cytosolic proteins (15–20 kDa) widely distributed in plants, fungi, and some animals. Initially identified as stress-inducible molecules in plant defense responses, they are upregulated during biotic stressors (e.g., pathogen attacks) and abiotic stressors (e.g., drought, temperature shifts). Structurally, PR-10 proteins feature a characteristic hydrophobic cavity formed by a curved β-sheet and α-helices, resembling the Bet v 1 fold. This cavity allows binding to diverse ligands, including phytohormones (e.g., cytokinins, brassinosteroids), flavonoids, and fatty acids, suggesting roles in signaling and detoxification.
Recombinant PR-10 proteins are engineered using heterologous expression systems (e.g., *E. coli*, yeast, or plant cell cultures*) for functional and biomedical studies. Their production enables detailed analysis of ligand interactions, enzymatic activities (e.g., ribonuclease or phosphatase-like functions), and immunogenic properties. Notably, PR-10 homologs like Bet v 1 (birch pollen allergen) and Mal d 1 (apple allergen) are major triggers of human allergic reactions, making recombinant forms valuable for allergy diagnostics, epitope mapping, and hypoallergenic vaccine development.
Research on recombinant PR-10 proteins also explores their biotechnological potential, such as enhancing plant stress tolerance through genetic engineering or developing antimicrobial agents. However, challenges persist, including protein solubility issues during expression and functional variability across species. Recent studies leverage structural biology tools (e.g., X-ray crystallography, NMR) to dissect structure-function relationships and engineer optimized variants for targeted applications. Overall, PR-10 recombinant proteins serve as critical tools in understanding plant-pathogen interactions, allergy mechanisms, and stress adaptation biology.
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