| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | PHLPI |
| Uniprot No | P43213 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-263aa |
| 氨基酸序列 | IPKVPPGPNITATYGDKWLDAKSTWYGKPTGAGPKDNGGACGYKDVDKPPFSGMTGCGNTPIFKSGRGCGSCFEIKCTKPEACSGEPVVVHITDDNEEPIAPYHFDLSGHAFGAMAKKGDEQKLRSAGELELQFRRVKCKYPEGTKVTFHVEKGSNPNYLALLVKYVNGDGDVVAVDIKEKGKDKWIELKESWGAIWRIDTPDKLTGPFTVRYTTEGGTKTEAEDVIPEGWKADTSYESK |
| 预测分子量 | 39.2 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PHLPI重组蛋白的3篇虚构参考文献示例，格式为文献名称、作者和摘要概括：
1. **"Efficient expression and purification of recombinant PHLPI protein in E. coli"**
- Authors: Zhang L, Wang Y, Chen H
- 摘要：研究报道了一种通过大肠杆菌系统高效表达PHLPI重组蛋白的方法，优化了诱导条件与纯化工艺，获得高纯度蛋白并验证其生物活性。
2. **"PHLPI recombinant protein inhibits tumor growth via modulating cellular signaling pathways"**
- Authors: Smith J, Tanaka R, Gupta S
- 摘要：通过体外和动物实验证明PHLPI重组蛋白通过抑制PI3K/AKT和MAPK通路抑制癌细胞增殖，并显著降低小鼠模型中肿瘤体积。
3. **"Structural and functional characterization of PHLPI as a novel immune regulator"**
- Authors: Kim D, Müller F, Li X
- 摘要：利用X射线晶体学解析了PHLPI重组蛋白的三维结构，结合功能实验揭示其通过结合特定免疫细胞受体调控炎症反应的分子机制。
注：以上文献为示例性质，实际研究中请以具体数据库(如PubMed、Web of Science)检索结果为准。若需真实文献，请提供更准确的蛋白名称或相关研究领域信息。
**Background of Recombinant PHL pI Protein**
The recombinant PHL pI protein is derived from *Platanus hispanica* (London plane tree), a common source of allergenic pollen linked to seasonal respiratory allergies. PHL pI, a major allergen in this species, belongs to the pathogenesis-related (PR-10) protein family, characterized by a conserved Bet v 1-like structure. These proteins are implicated in plant defense mechanisms but also act as potent allergens due to their ability to bind immunoglobulin E (IgE) in sensitized individuals.
The production of recombinant PHL pI emerged to address challenges in studying and diagnosing allergies caused by natural pollen extracts. Traditional extracts vary in allergen composition and stability, complicating standardization for research or clinical use. Recombinant technology enables the expression of PHL pI in controlled systems (e.g., *E. coli* or yeast), ensuring high purity, consistency, and scalability. This approach bypasses seasonal and geographical limitations of natural allergen collection.
Recombinant PHL pI is pivotal in allergy diagnostics, facilitating precise IgE reactivity profiling to improve personalized treatment strategies. It also serves as a tool for studying cross-reactivity with homologous allergens (e.g., Bet v 1 from birch pollen), a common issue in pollen-food syndrome. Additionally, it holds promise for allergen-specific immunotherapy (AIT), where modified hypoallergenic variants can be engineered to reduce adverse reactions while retaining immunomodulatory properties.
Research on recombinant PHL pI has advanced understanding of PR-10 allergenicity, including structural epitopes and immune interactions. Its application supports the development of component-resolved diagnostics and next-generation therapeutics, offering safer, standardized alternatives to conventional allergy management. This innovation underscores the integration of molecular biology in tackling allergenic diseases, enhancing both scientific and clinical outcomes.
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