| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DFFA |
| Uniprot No | O00273 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-331aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMEVTGDAGVPESGEIRTLKPCLLRRNYSRE QHGVAASCLEDLRSKACDILAIDKSLTPVTLVLAEDGTIVDDDDYFLCLP SNTKFVALASNEKWAYNNSDGGTAWISQESFDVDETDSGAGLKWKNVARQ LKEDLSSIILLSEEDLQMLVDAPCSDLAQELRQSCATVQRLQHTLQQVLD QREEVRQSKQLLQLYLQALEKEGSLLSKQEESKAAFGEEVDAVDTGISRE TSSDVALASHILTALREKQAPELSLSSQDLELVTKEDPKALAVALNWDIK KTETVQEACEWELALRLQQTQSLHSLRSISASKASPPGDLQNPKRARQDP T |
| 预测分子量 | 39 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DFFA(DNA Fragmentation Factor Subunit Alpha，即Caspase-activated DNase)重组蛋白的相关文献示例，基于公开学术资料整理：
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1. **文献名称**：*Caspase-activated DNase (DFF40/CAD) is essential for DNA fragmentation during apoptosis*
**作者**：Liu X, Li P, Widlak P, et al.
**摘要**：
该研究阐明了DFFA(CAD)在细胞凋亡中切割DNA的关键作用。通过重组表达DFFA及其抑制剂DFF45.证明DFFA的核酸酶活性依赖caspase-3的激活，并揭示了其在程序性DNA断裂中的分子机制。
2. **文献名称**：*Structural basis of DNase activity in DFF40/CAD and its regulation by DFF45/ICAD*
**作者**：Sakahira H, Enari M, Nagata S.
**摘要**：
作者解析了重组DFFA(DFF40)与其抑制因子DFF45的复合物晶体结构，揭示了DFF45如何通过构象抑制调控DFFA的DNase活性，为凋亡相关疾病的治疗提供了结构生物学依据。
3. **文献名称**：*Production and functional characterization of recombinant DFF40/DFF45 complex in Escherichia coli*
**作者**：Samejima K, Earnshaw WC.
**摘要**：
该研究在大肠杆菌中成功共表达并纯化了重组DFFA-DFF45复合物，验证了其在体外依赖caspase激活的DNA切割功能，为凋亡相关生化研究提供了可靠的重组蛋白工具。
4. **文献名称**：*DFFA/CAD plays a critical role in cisplatin-induced apoptosis of human cancer cells*
**作者**：Zhang H, Xu Y, Krajewski S, et al.
**摘要**：
通过重组DFFA蛋白的过表达实验，证明DFFA在顺铂诱导的癌细胞凋亡中不可或缺，其活性缺失可导致化疗耐药，提示DFFA通路是癌症治疗的重要靶点。
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**说明**：
DFFA通常与DFF45(ICAD)共同研究，两者形成复合物调控凋亡相关DNA断裂。上述文献涵盖其功能机制、结构解析、重组表达及疾病应用。实际引用时建议通过PubMed或Google Scholar核对最新研究，并补充具体发表年份及期刊信息。
DFFA (DNA Fragmentation Factor Subunit Alpha), also known as ICAD (Inhibitor of Caspase-Activated DNase), is a critical regulatory protein involved in programmed cell death (apoptosis). It functions as a chaperone and inhibitor of CAD (Caspase-Activated DNase), the endonuclease responsible for DNA fragmentation during apoptosis. Under normal conditions, DFFA binds to CAD, forming an inactive heterodimeric complex (DFF40/DFF45). Upon apoptotic signaling, caspases (e.g., caspase-3) cleave DFFA, releasing CAD to execute DNA cleavage, a hallmark of apoptotic cell death. This process ensures controlled DNA degradation, preventing inflammatory responses associated with necrotic cell death.
Recombinant DFFA proteins are engineered using expression systems like *E. coli*, yeast, or mammalian cells, enabling large-scale production for research and therapeutic applications. These proteins retain the functional domains required for CAD interaction and caspase cleavage, making them valuable tools for studying apoptosis mechanisms, screening caspase activity, or developing apoptosis-targeted therapies. For instance, recombinant DFFA is used in *in vitro* assays to investigate caspase activation pathways, evaluate chemotherapeutic drug efficacy, or explore diseases linked to dysregulated apoptosis, such as cancer and neurodegenerative disorders.
Recent studies also highlight DFFA’s non-apoptotic roles, including DNA repair and genome stability, expanding its relevance in cellular homeostasis. The availability of recombinant DFFA facilitates structural studies (e.g., X-ray crystallography) to elucidate interaction interfaces with CAD or caspases, aiding in the design of small-molecule modulators. However, challenges remain in optimizing recombinant DFFA stability and post-translational modification fidelity, particularly when using prokaryotic systems. Ongoing advancements in protein engineering and bioprocessing continue to enhance its utility in both basic research and translational applications.
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