| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PARP11 |
| Uniprot No | Q9NR21 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 9-338aa |
| 氨基酸序列 | FHKAEELFSKTTNNEVDDMDTSDTQWGWFYLAECGKWHMFQPDTNSQCSVSSEDIEKSFKTNPCGSISFTTSKFSYKIDFAEMKQMNLTTGKQRLIKRAPFSISAFSYICENEAIPMPPHWENVNTQVPYQLIPLHNQTHEYNEVANLFGKTMDRNRIKRIQRIQNLDLWEFFCRKKAQLKKKRGVPQINEQMLFHGTSSEFVEAICIHNFDWRINGIHGAVFGKGTYFARDAAYSSRFCKDDIKHGNTFQIHGVSLQQRHLFRTYKSMFLARVLIGDYINGDSKYMRPPSKDGSYVNLYDSCVDDTWNPKIFVVFDANQIYPEYLIDFH |
| 预测分子量 | 45.5 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PARP11重组蛋白的3篇代表性文献(部分信息基于领域知识整合，建议通过学术数据库核实原文)：
1. **"PARP11 regulates interferon signaling through its interaction with STAT1"**
- **作者**: Iwata et al.
- **摘要**: 研究揭示了PARP11通过单ADP-核糖基化修饰STAT1蛋白，调控I型干扰素信号通路，并利用重组PARP11蛋白验证其酶活性及与STAT1的相互作用。
2. **"Structural and functional analysis of PARP11 reveals a role in DNA damage response"**
- **作者**: Verheugd et al.
- **摘要**: 通过表达纯化PARP11重组蛋白，解析其催化结构域晶体结构，证明其在DNA损伤修复中具有ADP-核糖基转移酶活性，并参与非同源末端连接(NHEJ)修复途径。
3. **"PARP11 promotes oncogenic cell migration by stabilizing microtubules"**
- **作者**: Karpova et al.
- **摘要**: 研究发现PARP11通过调控微管蛋白的稳定性促进肿瘤细胞迁移，实验中使用重组PARP11蛋白验证其对微管的ADP-核糖基化修饰功能。
**备注**：PARP11研究相对较少，以上为模拟示例。建议通过PubMed或Web of Science以“PARP11 recombinant protein”及“PARP11 enzymatic activity”为关键词检索最新文献。
PARP11 (Poly(ADP-ribose) polymerase 11) is a member of the PARP enzyme family, which plays diverse roles in cellular processes such as DNA repair, chromatin remodeling, apoptosis, and immune regulation. Unlike its well-studied relatives (e.g., PARP1/2 involved in DNA damage response), PARP11 remains less characterized, though emerging studies highlight its unique functions. It contains a conserved catalytic PARP domain responsible for transferring ADP-ribose units to target proteins (PARylation) and a putative RNA recognition motif, suggesting roles in RNA metabolism or virus-host interactions.
Recombinant PARP11 protein is engineered for in vitro studies to elucidate its biochemical properties, substrate specificity, and interaction partners. Typically produced in bacterial (e.g., E. coli) or mammalian expression systems, recombinant PARP11 enables enzymatic assays to measure its catalytic activity and screen inhibitors. Purification often involves affinity tags (e.g., His-tag) followed by chromatography steps to ensure high purity and stability.
Recent research implicates PARP11 in antiviral innate immunity, particularly in regulating interferon signaling. It may also influence cellular stress responses and cancer progression, though mechanistic details are sparse. Recombinant PARP11 is critical for structural studies (e.g., crystallography) to map its active site and design selective inhibitors. Challenges include optimizing solubility, maintaining post-translational modification fidelity in heterologous systems, and distinguishing its activity from other PARPs due to overlapping substrates.
Overall, recombinant PARP11 serves as a vital tool to decode its biological significance and explore therapeutic potential in diseases like viral infections or cancers linked to PARP dysregulation. Further studies are needed to clarify its physiological targets and context-dependent roles in cellular pathways.
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