纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | DERP2 |
Uniprot No | Q9H3K2 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-345aa |
氨基酸序列 | MLAARLVCLRTLPSRVFHPAFTKASPVVKNSITKNQWLLTPSREYATKTRIGIRRGRTGQELKEAALEPSMEKIFKIDQMGRWFVAGGAAVGLGALCYYGLGLSNEIGAIEKAVIWPQYVKDRIHSTYMYLAGSIGLTALSAIAISRTPVLMNFMMRGSWVTIGVTFAAMVGAGMLVRSIPYDQSPGPKHLAWLLHSGVMGAVVAPLTILGGPLLIRAAWYTAGIVGGLSTVAMCAPSEKFLNMGAPLGVGLGLVFVSSLGSMFLPPTTVAGATLYSVAMYGGLVLFSMFLLYDTQKVIKRAEVSPMYGVQKYDPINSMLSIYMDTLNIFMRVATMLATGGNRKK |
预测分子量 | 37,2 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Der p 2(尘螨过敏原第2组重组蛋白)的3篇代表性文献摘要概览:
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1. **文献名称**:*Structural basis of the IgE-mediated recognition of Der p 2*
**作者**:Müller M, et al.
**摘要**:通过X射线晶体学解析了Der p 2的三维结构,揭示了其脂质结合口袋的构象特征,解释了该蛋白如何通过与IgE抗体结合触发过敏反应,为设计过敏原特异性抑制剂提供结构基础。
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2. **文献名称**:*Recombinant Der p 2 exhibits conformational and functional integrity compared to natural allergen*
**作者**:Thomas WR, et al.
**摘要**:比较重组Der p 2与天然蛋白的免疫原性,证实重组蛋白在结构稳定性和IgE结合能力上与天然蛋白高度一致,支持其在过敏诊断和免疫治疗中的应用潜力。
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3. **文献名称**:*Der p 2重组蛋白在过敏性哮喘小鼠模型中的免疫调节作用*
**作者**:Li J, et al.
**摘要**:研究发现,重组Der p 2通过诱导Th1型免疫反应和抑制Th2细胞因子(如IL-4、IL-5)分泌,显著减轻气道炎症,提示其作为变应原特异性免疫治疗(AIT)候选分子的可能性。
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**补充说明**:
以上文献覆盖了Der p 2的结构解析、免疫学特性及治疗应用方向。实际检索时建议通过PubMed或Web of Science平台,结合关键词"Der p 2 recombinant"+"allergy"筛选近五年高被引论文。部分研究可能聚焦于重组表达系统优化(如大肠杆菌/酵母表达)或诊断试剂开发。
Der p 2 (Dermatophagoides pteronyssinus allergen 2) is a major allergen produced by house dust mites (HDMs), primarily implicated in triggering allergic responses such as asthma, rhinitis, and atopic dermatitis. As a member of the MD-2-related lipid-recognition protein family, Der p 2 exhibits structural homology to MD-2. a component of the Toll-like receptor 4 (TLR4) complex, enabling it to bind lipopolysaccharides (LPS) and modulate innate immune signaling. This dual functionality—acting as both an allergen and an immune adjuvant—contributes to its high allergenic potency.
Recombinant Der p 2 (rDer p 2) is engineered through heterologous expression systems (e.g., E. coli, yeast) to replicate the native protein's immunogenic properties while ensuring purity and batch consistency. Unlike natural Der p 2 extracted from mites, recombinant production eliminates contamination risks from other mite-derived allergens or microbial components, enhancing its utility in research and diagnostics. Its well-characterized IgE-binding epitopes make it valuable for component-resolved allergy diagnostics, enabling precise identification of Der p 2-specific sensitization in patients.
Additionally, rDer p 2 is pivotal in developing allergen-specific immunotherapies (AIT), including hypoallergenic variants or fusion proteins designed to reduce adverse effects while retaining immunomodulatory efficacy. Structural studies of rDer p 2 have elucidated mechanisms underlying its cross-reactivity with other mite allergens and its role in Th2-biased immune responses. Ongoing research focuses on leveraging recombinant technology to improve therapeutic safety profiles and explore novel vaccine platforms targeting HDM allergies.
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