| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DDA1 |
| Uniprot No | Q9BW61 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-102aa |
| 氨基酸序列 | ADFLKGLPVYNKSNFSRFHADSVCKASNRRPSVYLPTREYPSEQIIVTEKTNILLRYLHQQWDKKNAAKKRDQEQVELEGESSAPPRKVARTDSPDMHEDT |
| 预测分子量 | 17.7 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. |
以下是假设的关于DDA1重组蛋白的参考文献示例(注：文献为虚构，仅供格式参考)：
1. **《Expression and Purification of Recombinant DDA1 Protein in E. coli》**
- 作者：Zhang et al.
- 摘要：本研究通过构建DDA1基因的原核表达载体，在大肠杆菌中成功表达并纯化重组DDA1蛋白，优化了表达条件以提高蛋白产量，为后续功能研究提供材料。
2. **《DDA1 Interacts with VHL Protein to Regulate HIF-1α Degradation》**
- 作者：Müller et al.
- 摘要：探讨DDA1重组蛋白与VHL(von Hippel-Lindau)肿瘤抑制蛋白的相互作用，揭示其在HIF-1α泛素化降解途径中的调控作用，可能参与癌症发生机制。
3. **《Structural Characterization of DDA1 by X-ray Crystallography》**
- 作者：Tanaka et al.
- 摘要：通过X射线晶体学解析重组DDA1蛋白的三维结构，发现其具有典型的泛素连接酶复合体亚基特征，并预测其与CUL4A蛋白的结合位点。
4. **《Functional Analysis of Recombinant DDA1 in DNA Damage Response》**
- 作者：Li & Chen
- 摘要：利用重组DDA1蛋白进行体外实验，证明其通过调控CRL4泛素连接酶复合体活性参与DNA损伤修复，为靶向治疗提供潜在策略。
(注：以上文献为模拟内容，实际研究中请替换为真实发表的文献。)
DDA1 (Damage-specific DNA-binding protein 1-associated protein 1) is a ubiquitously expressed protein involved in the ubiquitin-proteasome system (UPS), a critical pathway for targeted protein degradation in eukaryotic cells. Initially identified as a binding partner of DDB1. a key component of the CUL4-DDB1 E3 ubiquitin ligase complex, DDA1 plays a regulatory role in substrate recognition and ubiquitination processes. Structurally, DDA1 contains a conserved DDA1 domain that facilitates interactions with other proteins, including CRBN (Cereblon), a substrate receptor in the CRL4 E3 ligase complex. This interaction highlights its role in mediating protein-protein interactions essential for substrate specificity during ubiquitination.
Recombinant DDA1 protein is engineered using expression systems like *E. coli* or mammalian cells, enabling studies of its biochemical properties and molecular functions. Its production often involves affinity tags (e.g., His-tag) for purification, ensuring high purity and activity. Research has linked DDA1 to diverse cellular processes, including DNA damage repair, cell cycle regulation, and apoptosis. Overexpression or dysregulation of DDA1 has been observed in certain cancers, suggesting its potential as a therapeutic target or biomarker.
In drug discovery, recombinant DDA1 aids in elucidating mechanisms of ubiquitin-mediated proteolysis, particularly in developing proteolysis-targeting chimeras (PROTACs) and other UPS-targeted therapies. Structural studies using recombinant DDA1 have provided insights into its binding interfaces and conformational changes during ligase assembly. Additionally, it serves as a tool to explore interactions with viral proteins, revealing strategies pathogens use to hijack host UPS machinery. Overall, DDA1 recombinant protein is a vital resource for advancing understanding of cellular protein homeostasis and its implications in disease.
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