| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | DERF2 |
| Uniprot No | Q00855 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 18-146aa |
| 氨基酸序列 | DQVDVKDCANNEIKKVMVDGCHGSDPCIIHRGKPFTLEALFDANQNTKTAKIEIKASLDGLEIDVPGIDTNACHFMKCPLVKGQQYDIKYTWNVPKIAPKSENVVVTVKLIGDNGVLACAIATHGKIRD |
| 预测分子量 | 16.1 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DERF2重组蛋白的示例参考文献(内容为虚构示例，仅供参考)：
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1. **文献名称**: *Heterologous Expression and Functional Analysis of DERF2 in Arabidopsis thaliana*
**作者**: Zhang, L., et al.
**摘要**: 本研究在大肠杆菌中成功表达并纯化了DERF2重组蛋白，通过转基因拟南芥验证其作为乙烯响应因子的功能，证明DERF2通过调控下游胁迫响应基因增强植物耐旱性。
2. **文献名称**: *Crystal Structure of DERF2 Reveals DNA-Binding Specificity*
**作者**: Chen, X., & Wang, H.
**摘要**: 报道DERF2重组蛋白的晶体结构解析，揭示其AP2结构域与靶DNA结合的分子机制，为设计植物抗逆基因工程提供结构基础。
3. **文献名称**: *DERF2 Recombinant Protein Enhances Pathogen Resistance in Rice*
**作者**: Liu, Y., et al.
**摘要**: 通过原核系统表达DERF2重组蛋白，证实其体外结合病原相关启动子元件的能力，并提高水稻对稻瘟病的抗性，提示其在植物免疫中的调控作用。
4. **文献名称**: *Optimization of DERF2 Expression in Pichia pastoris for Biotechnological Applications*
**作者**: Kim, S., et al.
**摘要**: 优化毕赤酵母中DERF2重组蛋白的高效分泌表达，展示其在农业生物技术中作为抗逆诱导剂的潜在应用价值。
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注：以上文献为示例性内容，实际研究中请通过学术数据库(如PubMed、Web of Science)检索真实文献。
DERF2 recombinant protein is derived from *Dermatophagoides farinae*, a common house dust mite species implicated in allergic diseases such as asthma, rhinitis, and atopic dermatitis. As a major allergen in mite extracts, Der f 2 (Dermatophagoides farinae allergen 2) belongs to the Group 2 mite allergen family, which shares structural and functional homology with lipid-binding proteins. These allergens trigger IgE-mediated immune responses in sensitized individuals, contributing to chronic inflammation and allergic symptoms.
Structurally, Der f 2 is a 14-16 kDa globular protein characterized by a unique β-barrel fold stabilized by three conserved disulfide bonds. Its stability and resistance to environmental degradation enhance allergenicity. Recombinant DERF2 is produced using expression systems like *Escherichia coli* or yeast, enabling precise control over purity and batch consistency compared to natural extracts. This recombinant form retains the immunodominant epitopes required for IgE recognition, making it valuable for diagnostic and therapeutic applications.
Research on DERF2 focuses on elucidating its role in allergic sensitization, cross-reactivity with other Group 2 allergens (e.g., Der p 2 from *Dermatophagoides pteronyssinus*), and interactions with immune receptors like TLR4. Clinically, recombinant DERF2 is used in component-resolved diagnostics to identify mite-specific allergies and in allergen-specific immunotherapy (AIT) formulations to induce immune tolerance. Its standardized production reduces variability in allergy testing and improves safety profiles in AIT. Ongoing studies explore engineered hypoallergenic variants and combination therapies targeting multiple mite allergens to enhance treatment efficacy.
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