| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DERP3 |
| Uniprot No | P39675 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-261aa |
| 氨基酸序列 | MIIYNILIVLLLAINTLANPILPASPNATIVGGEKALAGECPYQISLQSSSHFCGGTILDEYWILTAAHCVAGQTASKLSIRYNSLKHSLGGEKISVAKIFAHEKYDSYQIDNDIALIKLKSPMKLNQKNAKAVGLPAKGSDVKVGDQVRVSGWGYLEEGSYSLPSELRRVDIAVVSRKECNELYSKANAEVTDNMICGGDVANGGKDSCQGDSGGPVVDVKNNQVVGIVSWGYGCARKGYPGVYTRVGNFIDWIESKRSQ |
| 预测分子量 | 28,0 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. |
以下为关于DERP3(Der p 3)重组蛋白的模拟参考文献示例，内容基于真实研究领域方向，具体文献需通过学术数据库核实：
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1. **文献名称**: "Expression and Characterization of Recombinant Der p 3 Protease from *Dermatophagoides pteronyssinus*"
**作者**: Smith, J.L. et al.
**摘要**: 研究利用大肠杆菌表达系统成功重组表达Der p 3蛋白，并验证其酶活性。结果显示重组蛋白具有与天然过敏原相似的蛋白酶活性，可用于过敏原特异性IgE结合分析。
2. **文献名称**: "Structural Insights into Der p 3 Allergen and Its Role in Mite-Induced Asthma"
**作者**: Chen, H. & Mueller, G.A.
**摘要**: 通过X射线晶体学解析Der p 3的三维结构，揭示其半胱氨酸蛋白酶活性位点及与免疫球蛋白E(IgE)的结合表位，为设计过敏原特异性免疫疗法提供依据。
3. **文献名称**: "Evaluation of Recombinant Der p 3 for Clinical Diagnosis of Dust Mite Allergy"
**作者**: Wang, Y. et al.
**摘要**: 比较重组Der p 3与天然提取蛋白在过敏患者血清IgE检测中的效能，证明重组蛋白灵敏度达90%，且批次稳定性更优，适用于标准化过敏诊断试剂开发。
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**注**: Der p 3是尘螨(*Dermatophagoides pteronyssinus*)的主要过敏原之一，属于半胱氨酸蛋白酶家族，重组蛋白研究多聚焦于表达优化、免疫诊断及结构功能分析。实际文献请通过PubMed或Google Scholar检索关键词(如 "Der p 3 recombinant")获取。
**Background of DERP3 Recombinant Protein**
Der p 3. a major allergen from the house dust mite *Dermatophagoides pteronyssinus*, belongs to the serine protease family and is classified as a Group 3 mite allergen. It is a well-characterized component implicated in allergic diseases, such as asthma, rhinitis, and atopic dermatitis. Structurally, Der p 3 is a 30 kDa protein with enzymatic activity, functioning as a trypsin-like protease that contributes to its allergenicity by disrupting epithelial barriers, enhancing antigen penetration, and modulating immune responses. Its protease activity also interacts with other mite allergens (e.g., Der p 1 and Der p 2), amplifying inflammatory cascades in sensitized individuals.
Recombinant Der p 3 (rDer p 3) is produced via genetic engineering, typically using expression systems like *Escherichia coli*, yeast, or mammalian cells, to ensure proper folding and post-translational modifications. The development of recombinant Der p 3 addresses challenges in purifying native allergens from mite extracts, which are often contaminated with variable mixtures of proteins, microbes, or endotoxins. Recombinant technology enables standardized, scalable production of pure, consistent allergen batches, critical for diagnostic and therapeutic applications.
In research, rDer p 3 is used to study IgE-mediated immune responses, epitope mapping, and cross-reactivity with other allergens. Clinically, it serves as a key component in allergy diagnostics (e.g., IgE reactivity tests) and immunotherapy, including hypoallergenic variants engineered to reduce side effects while retaining immunogenicity. Despite its utility, challenges remain in mimicking the native protein’s conformational structure and enzymatic activity, which are essential for functional studies. Overall, rDer p 3 represents a vital tool for advancing allergy mechanisms, diagnostics, and targeted therapies.
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