| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | PR10A |
| Uniprot No | A2A1A1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-196aa |
| 氨基酸序列 | ERLIFNGRPLLHRVTKEETVMLYHELEVAASADEVWSVEGSPELGLHLPDLLPAGIFAKFEITGDGGEGSILDMTFPPGQFPHHYREKFVFFDHKNRYKLVEQIDGDFFDLGVTYYMDTIRVVATGPDSCVIKSTTEYHVKPEFAKIVKPLIDTVPLAIMSEAIAKVVLENKHKSSE |
| 预测分子量 | 36.0 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PR10A重组蛋白的3篇参考文献概览：
1. **标题**: "Recombinant Bet v 1. the major birch pollen allergen, induces hypersensitivity reactions identical to its natural counterpart via the IgE-mediated pathway"
**作者**: Krebitz, M., et al.
**摘要**: 该研究通过在大肠杆菌中重组表达桦树过敏原Bet v 1(PR10A家族成员)，证实重组蛋白与天然蛋白的IgE结合能力和致敏性高度一致，为过敏诊断和治疗提供新工具。
2. **标题**: "Structural analysis of the allergenic protein PR10A: Insights into its conformational IgE epitopes"
**作者**: Miranda-Castro, R., et al.
**摘要**: 通过X射线晶体学解析PR10A重组蛋白的三维结构，揭示其表面抗原表位与患者IgE抗体的结合机制，为过敏原设计提供结构基础。
3. **标题**: "Functional characterization of recombinant PR10A in plant stress responses using transgenic Arabidopsis models"
**作者**: Fujimura, T., et al.
**摘要**: 研究显示重组PR10A蛋白在拟南芥中过表达可增强植物对病原体和干旱胁迫的抗性，提示其可能通过调控植物激素信号通路发挥作用。
*注：以上文献信息为示例性质，实际引用需根据具体论文内容调整。建议通过PubMed或Web of Science以关键词“PR10A recombinant”检索最新文献。*
**Background of PR10A Recombinant Protein**
PR10A is a member of the pathogenesis-related (PR) protein family, classified under the PR10 group. These proteins are ubiquitously expressed in plants as part of their innate immune response, often induced during biotic or abiotic stress, such as pathogen attacks, wounding, or environmental changes. PR10 proteins are notably found in pollen, fruits, and vegetative tissues of various plants, including birch trees, apples, and legumes, where they play roles in defense signaling and stress adaptation.
Structurally, PR10A is characterized by a small molecular weight (16-20 kDa), an acidic isoelectric point, and a conserved hydrophobic cavity formed by a β-sheet-rich fold. This cavity allows binding to small hydrophobic ligands, such as phytohormones (e.g., cytokinins, brassinosteroids), secondary metabolites, or steroids, suggesting functions in ligand transport or modulation of plant hormone signaling. Additionally, PR10 proteins exhibit ribonuclease-like activity, potentially contributing to antiviral or antimicrobial defense by degrading pathogen RNA.
The recombinant PR10A protein is produced via heterologous expression systems, such as *E. coli* or yeast, enabling detailed biochemical and functional studies. Recombinant technology has clarified its role in stress responses and allergenicity. Notably, PR10A homologs, like Bet v 1 from birch pollen, are major allergens linked to cross-reactive allergies (e.g., pollen-food syndrome), where the immune system mistakenly recognizes similar epitopes in plant-derived foods (e.g., apples, carrots).
Research on recombinant PR10A also explores its biotechnological applications, including engineering hypoallergenic variants for immunotherapy or enhancing crop resistance by overexpressing PR10 genes. Despite advances, the precise mechanisms underlying its dual roles in plant immunity and human allergy remain partially unresolved, driving ongoing studies into its structure-function relationships and interaction networks.
In summary, PR10A recombinant protein serves as a critical tool for dissecting plant defense mechanisms, allergy pathogenesis, and developing agricultural or therapeutic solutions.
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