| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PARP |
| Uniprot No | P09874 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1014aa |
| 氨基酸序列 | MAESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVTGKGQDGIGSKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHPGCFVKNREELGFRPEYSASQLKGFSLLATEDKEALKKQLPGVKSEGKRKGDEVDGVDEVAKKKSKKEKDKDSKLEKALKAQNDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSGQLVFKSDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPKEFREISYLKKLKVKKQDRIFPPETSASVAATPPPSTASAPAAVNSSASADKPLSNMKILTLGKLSRNKDEVKAMIEKLGGKLTGTANKASLCISTKKEVEKMNKKMEEVKEANIRVVSEDFLQDVSASTKSLQELFLAHILSPWGAEVKAEPVEVVAPRGKSGAALSKKSKGQVKEEGINKSEKRMKLTLKGGAAVDPDSGLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKENRYWIFRSWGRVGTVIGSNKLEQMPSKEDAIEHFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQDEEAVKKLTVNPGTKSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAVSQGSSDSQILDLSNRFYTLIPHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSANISLDGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLLKLKFNFKTSLW |
| 预测分子量 | 113 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PARP重组蛋白的3篇示例参考文献(注：以下为虚构示例，仅用于演示格式)：
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1. **文献名称**: *"Expression and functional characterization of recombinant human PARP1 for DNA repair studies"*
**作者**: Thompson R., et al.
**摘要**: 研究报道了在大肠杆菌中高效表达并纯化重组人源PARP1蛋白的方法，证实其具有体外催化PARylation活性，并用于DNA损伤修复机制的体外分析。
2. **文献名称**: *"Structural analysis of PARP2 catalytic domain using recombinant protein crystallography"*
**作者**: Garcia S., et al.
**摘要**: 通过重组表达PARP2催化结构域蛋白，解析其三维晶体结构，揭示了其底物结合口袋的独特构象，为选择性抑制剂设计提供依据。
3. **文献名称**: *"High-throughput screening platform for PARP inhibitors based on recombinant PARP3 enzymatic activity"*
**作者**: Chen L., et al.
**摘要**: 开发了一种基于重组PARP3蛋白酶活性的高通量筛选系统，用于快速评估候选化合物对PARP3的抑制效力和特异性。
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如需真实文献，建议通过PubMed或Google Scholar检索关键词(如“recombinant PARP protein expression”、“PARP1 purification”)，并筛选近年高引用研究。
**Background of PARP Recombinant Proteins**
Poly(ADP-ribose) polymerase (PARP) enzymes are a family of proteins critical for DNA repair, genomic stability, and cellular homeostasis. The most studied member, PARP1. plays a central role in detecting and repairing single-strand DNA breaks via the base excision repair pathway. Upon binding to DNA lesions, PARP catalyzes the synthesis of poly(ADP-ribose) (PAR) chains on target proteins, recruiting repair machinery and modulating chromatin structure. Dysregulation of PARP activity is linked to cancer, neurodegenerative disorders, and inflammatory diseases.
Recombinant PARP proteins are engineered in vitro using expression systems like *E. coli* or mammalian cells, enabling large-scale production for research and therapeutic applications. These proteins retain key functional domains: an N-terminal DNA-binding domain, an automodification domain, and a C-terminal catalytic domain responsible for PAR synthesis. Recombinant PARP is vital for studying DNA repair mechanisms, screening PARP inhibitors (e.g., olaparib, niraparib), and developing cancer therapies that exploit synthetic lethality, particularly in BRCA-mutated cancers.
PARP inhibitors (PARPi), which block enzymatic activity, have revolutionized oncology by selectively targeting cancer cells with defective homologous recombination repair. Recombinant PARP proteins are also used to investigate resistance mechanisms, optimize inhibitor design, and explore PARP's roles beyond DNA repair, such as in transcription and apoptosis. Their versatility underscores their importance in both basic research and clinical translation.
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