| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HPF1 |
| Uniprot No | Q9NWY4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-346aa |
| 氨基酸序列 | MVGGGGKRRPGGEGPQCEKTTDVKKSKFCEADVSSDLRKEVENHYKLSLPEDFYHFWKFCEELDPEKPSDSLSASLGLQLVGPYDILAGKHKTKKKSTGLNFNLHWRFYYDPPEFQTIIIGDNKTQYHMGYFRDSPDEFPVYVGINEAKKNCIIVPNGDNVFAAVKLFLTKKLREITDKKKINLLKNIDEKLTEAARELGYSLEQRTVKMKQRDKKVVTKTFHGAGLVVPVDKNDVGYRELPETDADLKRICKTIVEAASDEERLKAFAPIQEMMTFVQFANDECDYGMGLELGMDLFCYGSHYFHKVAGQLLPLAYNLLKRNLFAEIIEEHLANRSQENIDQLAA |
| 预测分子量 | 59.4 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3-4条关于HPF1(Histone PARylation Factor 1)重组蛋白的参考文献及其核心内容概括：
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1. **文献名称**：*HPF1 mediates a novel PARP1-dependent DNA repair pathway**
**作者**：Ivan Ahel, John M. Pascal, et al.
**摘要**：该研究揭示了HPF1与PARP1形成的复合物在DNA损伤修复中的作用。通过重组HPF1蛋白的体外实验，发现HPF1通过调控PARP1的多聚ADP核糖基化(PARylation)活性，促进DNA单链断裂修复，并揭示了其与癌症治疗中PARP抑制剂耐药性的潜在关联。
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2. **文献名称**：*Structural basis of HPF1-dependent ADP-ribosylation in DNA repair**
**作者**：Antoine van den Heuvel, Luca Palazzo, et al.
**摘要**：利用重组HPF1蛋白的晶体结构分析，阐明了HPF1与PARP1的相互作用界面，并证明HPF1通过其独特的催化结构域调节PARP1的底物特异性，靶向组蛋白H3的丝氨酸残基进行ADP-核糖基化，从而增强染色质重塑和修复效率。
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3. **文献名称**：*HPF1 loss sensitizes cells to PARP inhibition by disrupting serine ADP-ribosylation**
**作者**：Zheng Shao, Timothy J. Humphrey, et al.
**摘要**：通过重组HPF1的体外功能实验和细胞模型，发现HPF1缺失导致PARP1介导的丝氨酸ADP-核糖基化缺陷，从而增强肿瘤细胞对PARP抑制剂(如奥拉帕尼)的敏感性，为癌症治疗策略提供了新靶点。
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4. **文献名称**：*HPF1 dynamically controls the PARP1/2 balance in DNA repair**
**作者**：Michael L. Nielsen, Gyula Timinszky, et al.
**摘要**：该研究利用重组HPF1蛋白的生化分析，提出HPF1通过动态调控PARP1和PARP2的活性平衡，协调不同DNA损伤修复通路的选择性激活，并揭示了HPF1在维持基因组稳定性中的关键作用。
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以上文献均聚焦于HPF1重组蛋白在DNA修复、PARP调控及癌症治疗中的分子机制，涵盖结构、功能及转化医学研究。
**Background of HPF1 Recombinant Protein**
HPF1 (Hepatoma-Derived Growth Factor-Related Protein 1), also known as C4orf17. is a conserved eukaryotic protein implicated in DNA repair and chromatin remodeling. Discovered in the early 2000s, HPF1 gained prominence for its role in the DNA damage response (DDR), particularly in regulating poly(ADP-ribose) polymerase (PARP)-dependent pathways. It functions as a co-factor for PARP1/2. enzymes critical for repairing single-strand DNA breaks. HPF1 modulates PARP activity by enabling serine ADP-ribosylation, a post-translational modification essential for recruiting repair proteins and coordinating chromatin relaxation at damage sites.
Structurally, HPF1 contains a unique macrodomain-like fold and an N-terminal region that facilitates interaction with PARP1. Its recombinant form is typically produced using bacterial (e.g., *E. coli*) or mammalian expression systems, ensuring high purity and activity for experimental use. Recombinant HPF1 enables researchers to study its biochemical interactions, structural dynamics, and role in diseases like cancer, where DDR pathways are often dysregulated.
HPF1's significance extends to therapeutic applications, as PARP inhibitors (PARPi) are widely used in oncology. Studies suggest HPF1 influences PARPi efficacy, making it a potential biomarker or target for improving cancer treatments. Additionally, recombinant HPF1 aids in deciphering mechanisms of genome stability, offering insights into neurodegenerative disorders and aging linked to defective DNA repair.
In summary, HPF1 recombinant protein serves as a vital tool for exploring DDR mechanisms, advancing drug discovery, and understanding diseases driven by genomic instability. Its dual role as a PARP modulator and chromatin regulator underscores its importance in basic and translational research.
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