| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ypr-10 |
| Uniprot No | D1YSM5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-157aa |
| 氨基酸序列 | MGAITYDMEIPSSISAEKMFKAFVLDGDTIIPKALPHAITGVQTLEGDGGVGTIKLTTFGEGSVHKSVKHRIDGLDKENFTYSYSIIEGGALDVFESISYHIKIVATPDGGCICKNRSIYTPKCDAQVSEEEIKAGKERASGIFKKVEAYLLANPDC |
| 预测分子量 | 32.9 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YPR-10重组蛋白的3篇代表性文献示例(注：内容为模拟虚构，实际文献需通过学术数据库查询)：
1. **文献名称**: *"Expression and antifungal activity of recombinant YPR-10 protein from Nicotiana tabacum"*
**作者**: Lee, S. et al.
**摘要**: 本研究克隆了烟草来源的YPR-10基因，在大肠杆菌中成功表达并纯化重组蛋白。体外实验表明，重组YPR-10对多种植物病原真菌(如灰霉菌)具有显著抑制活性，证实其参与植物先天免疫防御机制。
2. **文献名称**: *"Structural characterization of YPR-10 by X-ray crystallography reveals its RNase-like domain"*
**作者**: Zhang, Y. & Wang, H.
**摘要**: 通过X射线晶体学解析了重组YPR-10的三维结构，发现其具有典型的PR-10家族折叠模式及RNase-like活性位点。分子对接实验进一步揭示了其与RNA底物结合的潜在机制，为开发基于YPR-10的抗病毒药物提供结构基础。
3. **文献名称**: *"Allergenicity assessment of recombinant YPR-10 in birch pollen-related food allergy"*
**作者**: Müller, R. et al.
**摘要**: 评估了重组YPR-10与桦树花粉过敏原Bet v 1的交叉反应性。免疫印迹和患者血清IgE结合实验表明，YPR-10可能作为潜在食物过敏原，提示其在过敏性疾病诊断中的潜在应用价值。
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如需真实文献，建议检索PubMed或Web of Science，使用关键词“YPR-10”、“recombinant PR-10 protein”或结合具体物种(如马铃薯、辣椒等PR蛋白高表达植物)。
**Background of YPR-10 Recombinant Protein**
YPR-10 (pathogenesis-related protein 10) is a member of the PR-10 family, a group of small, intracellular proteins widely distributed in plants. These proteins are induced under biotic or abiotic stress, such as pathogen attacks, wounding, or environmental changes, and play critical roles in plant defense mechanisms. The PR-10 family is structurally characterized by a conserved Bet v 1-fold, a hydrophobic pocket that binds ligands like phytohormones or secondary metabolites, and ribonuclease (RNase) activity, which may contribute to antiviral or antimicrobial functions.
YPR-10. initially identified in potato (*Solanum tuberosum*), gained attention due to its dual role in plant immunity and allergenicity. Its homologs in other species, such as Bet v 1 (birch pollen allergen) and Pru av 1 (cherry allergen), are known allergens, linking PR-10 proteins to cross-reactive food-pollen allergy syndromes. Recombinant YPR-10 is produced via heterologous expression systems (e.g., *E. coli* or yeast) for functional and structural studies. Its production allows researchers to investigate its enzymatic activity, ligand-binding properties, and interaction with plant immune signaling pathways.
Studies highlight YPR-10’s involvement in jasmonic acid signaling and its potential as a biomarker for stress responses. Additionally, its allergenic properties make it a target for allergy diagnostics and immunotherapy research. The recombinant protein’s stability and solubility facilitate applications in biotechnology, including engineered disease-resistant crops and molecular tools for studying plant-pathogen interactions. Despite its significance, the exact mechanistic role of YPR-10 in defense and stress adaptation remains an active area of research, with ongoing efforts to elucidate its structure-function relationships and ecological relevance.
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