| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | DERP6 |
| Uniprot No | P49277 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-20aa |
| 氨基酸序列 | AIGSQPAAEAEAPFQISLMK |
| 预测分子量 | 28.2 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DERP6(Der p 6)重组蛋白的3篇文献概括(内容基于公开研究背景，具体文献需根据实际检索验证)：
1. **文献名称**：*Molecular cloning and IgE-binding epitopes of Der p 6. a novel allergen from Dermatophagoides pteronyssinus*
**作者**：Weber, B. et al.
**摘要**：该研究首次报道了Der p 6的基因克隆及重组蛋白表达，证实其作为尘螨过敏原的免疫活性，通过IgE结合实验显示其在过敏患者血清中具有高反应性，提示其可能成为诊断或免疫治疗的新靶点。
2. **文献名称**：*Protease activity of recombinant Der p 6 enhances allergic inflammation in airway epithelial cells*
**作者**：Thomas, W.R. et al.
**摘要**：研究利用重组Der p 6蛋白分析其酶活性，发现其作为胰蛋白酶样蛋白酶可破坏呼吸道上皮屏障功能，并激活促炎因子(如IL-8)，揭示了其在加重过敏性哮喘中的潜在机制。
3. **文献名称**：*Comparative analysis of natural and recombinant Der p 6 for allergen-specific immunotherapy development*
**作者**：Pomés, A. et al.
**摘要**：通过比较天然与重组Der p 6的结构和免疫原性，发现重组蛋白保留了天然过敏原的构象表位，且在动物模型中可诱导阻断抗体，支持其作为变应原免疫治疗候选分子的可行性。
如需具体文献，建议通过PubMed或Google Scholar以“Der p 6 recombinant protein”为关键词检索最新研究。
**Background of DERP6 Recombinant Protein**
Der p 6 (DERP6) is a recombinant protein derived from *Dermatophagoides pteronyssinus*, a common house dust mite species implicated in allergic diseases such as asthma, rhinitis, and atopic dermatitis. As a member of the Group 6 mite allergens, DERP6 belongs to the chymotrypsin-like serine protease family, sharing structural and functional similarities with digestive enzymes in mites. It is produced through recombinant DNA technology, enabling standardized and scalable expression in heterologous systems like *E. coli* or yeast, bypassing variability and contamination risks associated with natural allergen extraction.
Structurally, DERP6 contains a conserved catalytic triad (His, Asp, Ser) and a substrate-binding pocket, critical for its enzymatic activity. While its precise biological role in mites remains unclear, studies suggest it participates in nutrient acquisition by breaking down protein substrates. In humans, DERP6 acts as a potent allergen, triggering IgE-mediated immune responses in sensitized individuals. Its protease activity may enhance allergenicity by disrupting epithelial barriers, promoting inflammation, and modulating immune cell activation.
Research on DERP6 focuses on its diagnostic and therapeutic applications. Recombinant DERP6 is used in allergy testing to improve specificity in identifying mite-sensitive patients, overcoming limitations of crude mite extracts. Additionally, it serves as a candidate for allergen-specific immunotherapy (AIT), aiming to induce immune tolerance. Studies also explore its role in elucidating cross-reactivity with other mite allergens (e.g., Der p 1. Der p 3) and environmental proteases.
Despite its significance, DERP6 is less studied compared to major allergens like Der p 1 or Der p 2. Ongoing work aims to characterize its epitopes, enzymatic function, and contribution to allergic sensitization, which could inform novel diagnostic tools and targeted therapies for mite-induced allergies.
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