| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DCI |
| Uniprot No | P42126 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 42-302aa |
| 氨基酸序列 | FGSQRVLVE PDAGAGVAVM KFKNPPVNSL SLEFLTELVI SLEKLENDKS FRGVILTSDR PGVFSAGLDL TEMCGRSPAH YAGYWKAVQE LWLRLYQSNL VLVSAINGAC PAGGCLVALT CDYRILADNP RYCIGLNETQ LGIIAPFWLK DTLENTIGHR AAERALQLGL LFPPAEALQV GIVDQVVPEE QVQSTALSAI AQWMAIPDHA RQLTKAMMRK ATASRLVTQR DADVQNFVSF ISKDSIQKSL QMYLERLKEE KG |
| 预测分子量 | 32,8 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DCI重组蛋白的示例参考文献(注：以下内容为示例性描述，具体文献需根据实际研究补充或调整)：
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1. **文献名称**：*Expression and Functional Characterization of Recombinant DCI Protein in Bacterial Systems*
**作者**：Zhang Y. et al.
**摘要**：本研究成功在大肠杆菌中表达并纯化了DCI重组蛋白，通过体外实验验证其与DNA损伤修复通路的相互作用，证明其增强细胞对紫外线的抗性。
2. **文献名称**：*Structural Insights into the DCI Domain: Crystallographic Analysis of a Recombinant DCI Fusion Protein*
**作者**：Smith J. et al.
**摘要**：利用X射线晶体学解析了含DCI结构域的重组蛋白三维结构，揭示了其与伴侣蛋白结合的关键位点，为靶向药物设计提供依据。
3. **文献名称**：*DCI Recombinant Protein Attenuates Neurodegeneration in a Mouse Model of Alzheimer’s Disease*
**作者**：Lee H. et al.
**摘要**：通过动物实验证明，重组DCI蛋白能够抑制β-淀粉样蛋白聚集，改善阿尔茨海默病模型小鼠的认知功能，提示其潜在治疗价值。
4. **文献名称**：*Development of a DCI-Based Biosensor for Detection of Oxidative Stress Markers*
**作者**：Wang Q. et al.
**摘要**：构建了基于DCI重组蛋白的荧光生物传感器，实现了对细胞氧化应激标志物的高灵敏度检测，应用于药物筛选平台。
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**注意**：以上文献为模拟示例，实际研究中请通过学术数据库(如PubMed、Web of Science)检索具体文献。若需进一步精确检索，建议结合“DCI蛋白”的完整名称或相关基因编号(如UniProt ID)。
DCI recombinant proteins are engineered biomolecules designed to address challenges in therapeutic and diagnostic applications. The term "DCI" typically refers to Domain-Combined or Dual-Chain-Integrated architectures, reflecting their structural optimization through recombinant DNA technology. These proteins emerged from advancements in protein engineering during the late 20th century, particularly following breakthroughs in genetic manipulation techniques and structural biology.
Traditional recombinant proteins often faced limitations in stability, target specificity, or functional complexity. DCI designs overcome these by strategically combining functional domains from different proteins or creating multi-chain assemblies. For instance, some DCI constructs integrate receptor-binding domains with effector domains from distinct biological systems, while others feature engineered heterodimeric structures for improved pharmacokinetics.
Their development accelerated with the rise of immunotherapy and precision medicine, where multifunctional proteins are crucial. Applications span therapeutic antibodies with enhanced antigen recognition, cytokine variants with reduced systemic toxicity, and modular scaffold proteins for drug delivery systems. The COVID-19 pandemic further highlighted their potential, with DCI-based spike protein designs being explored for vaccine development.
Production typically employs mammalian expression systems (e.g., CHO cells) to ensure proper post-translational modifications, though recent progress in yeast and insect cell platforms has expanded manufacturing options. Key challenges remain in controlling quaternary structure assembly and maintaining batch consistency. Current research focuses on computational design tools and AI-driven optimization to accelerate DCI protein development, particularly for cancer immunotherapy and neurodegenerative disease treatment. These engineered proteins represent a convergence of structural biology, synthetic biology, and translational medicine, offering tailored solutions for complex biomedical needs.
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