| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | dda |
| Uniprot No | P32270 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-439aa |
| 氨基酸序列 | MTFDDLTEGQKNAFNIVMKAIKEKKHHVTINGPAGTGKTTLTKFIIEALISTGGTGIILAAPTHAAKKILSKLSGKEASTIHSILKINPVTYEENVLFEQKEVPDLAKCRVLICDEVSMYDRKLFKILLSTIPPWCTIIGIGDNKQIRPVEPGENTAYISPFFTHKDFYQCELTEVKRSNAPIIDVATDVRNGKWNYDKVVDGHGVRGFTGDTALRDFMVNYFSIVKSLDDLFENRVMAFTNKSVDKLNSIIRKKIFETDKDFIVGEIIVMQEPLFKTYKIDGKPVSEIIFNNGQLVRIIEAEYTSTFVKARGVPGEYLIRHWDLTVETYGDDEYYREKIKIISSDEELYKFNLFLAKTAETYKNWNKGGKAPWSDFWDAKSQFSKVKALPASTFHKAQGMSVDRAFIYTPCIHYADVELAQQLLYVGVTRGRYDVFYV |
| 预测分子量 | 54.0 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. |
以下是关于DDA重组蛋白的模拟参考文献示例(注：部分内容为假设性概括，建议通过学术数据库验证)：
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1. **文献名称**：*Recombinant Expression and Functional Analysis of DDAH-2 in Endothelial Dysfunction*
**作者**：Smith A, et al.
**摘要**：研究报道了人源DDAH-2(二甲基精氨酸二甲胺水解酶同工酶2)的重组表达及纯化，验证其通过调节一氧化氮合成通路改善内皮细胞功能障碍的作用，为心血管疾病治疗提供潜在靶点。
2. **文献名称**：*Development of a DDA/MPL Adjuvant System for Subunit Vaccines*
**作者**：Li J, et al.
**摘要**：探讨了基于重组DDA(二甲基三十六烷胺)脂质体与MPL(单磷酰脂质A)的佐剂系统，在结核疫苗中增强抗原递送和Th1免疫应答的效果，证明其在小鼠模型中的有效性。
3. **文献名称**：*Crystallization and Structural Characterization of Recombinant DDA from Archaea*
**作者**：Wang Y, et al.
**摘要**：首次报道了古菌来源的DDA蛋白(DNA依赖性ATP酶)的重组表达、结晶及三维结构解析，揭示其ATP水解活性机制，为核酸代谢研究提供新见解。
4. **文献名称**：*Enhancement of DDA1 Recombinant Protein Stability via Site-Directed Mutagenesis*
**作者**：Chen L, et al.
**摘要**：通过定点突变优化DDA1(泛素连接酶复合物组分)重组蛋白的稳定性，并验证其在体外泛素化实验中的功能，为癌症靶向治疗研究奠定基础。
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**备注**：以上文献为示例性质，具体研究需以实际检索结果为准。建议使用PubMed、Web of Science等平台，以“DDA recombinant protein”或相关关键词进行精准查询。若DDA指代特定蛋白缩写，需结合具体研究领域进一步筛选。
DDA (dimethyldioctadecylammonium) recombinant proteins represent a class of engineered biologics designed to enhance immune responses in vaccine development. DDA, a cationic lipid-based adjuvant, has been widely studied for its ability to form stable particles that efficiently deliver antigens to antigen-presenting cells (APCs). When combined with recombinant proteins—purified antigens produced via genetic engineering in heterologous systems like *E. coli* or yeast—DDA acts as a delivery vehicle and immunostimulant, improving antigen stability, cellular uptake, and cross-presentation.
The concept emerged from efforts to address limitations of traditional vaccines, such as weak T-cell activation or poor antigen persistence. Recombinant protein technology allows precise antigen design (e.g., subunit vaccines, viral epitopes), while DDA’s positively charged liposomes bind negatively charged proteins, forming nano/microparticles that mimic pathogen structures. This complex enhances dendritic cell recruitment and promotes both humoral and cell-mediated immunity, critical for combating intracellular pathogens (e.g., *Mycobacterium tuberculosis*) or cancers.
DDA-recombinant protein platforms gained traction in the 2000s, particularly for tuberculosis vaccines, where DDA’s Th1-skewing properties align with the need for robust cellular immunity. Recent studies explore its utility in cancer immunotherapy, HIV, and malaria. Advantages include improved safety over live-attenuated vaccines, tunable antigen-adjuvant ratios, and scalability. However, challenges like batch variability, storage stability, and optimizing charge interactions remain active research areas. Ongoing work focuses on hybrid systems incorporating TLR agonists or thermoresponsive polymers to further amplify immunogenicity, positioning DDA-recombinant proteins as versatile tools in next-generation vaccine design.
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