| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PARP16 |
| Uniprot No | Q8N5Y8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-287 aa |
| 活性数据 | MQPSGWAAAREAAGRDMLAADLRCSLFASALQSYKRDSVLRPFPASYARGDCKDFEALLADASKLPNLKELLQSSGDNHKRAWDLVSWILSSKVLTIHSAGKAEFEKIQKLTGAPHTPVPAPDFLFEIEYFDPANAKFYETKGERDLIYAFHGSRLENFHSIIHNGLHCHLNKTSLFGEGTYLTSDLSLALIYSPHGHGWQHSLLGPILSCVAVCEVIDHPDVKCQTKKKDSKEIDRRRARIKHSEGGDIPPKYFVVTNNQLLRVKYLLVYSQKPPKRASSQLSWFS |
| 分子量 | 39.1 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人PARP16蛋白的3篇代表性文献示例(注：文献信息需根据实际情况核实更新)：
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1. **文献名称**：*Mono-ADP-ribosylation by PARP16 inhibits protein kinase Cα catalytic activity*
**作者**：Di Paola S, et al.
**摘要**：本研究揭示了PARP16通过单ADP核糖基化修饰PKCα的C端调控其酶活性，影响细胞凋亡与肿瘤信号通路，为PARP16在癌症中的作用提供新机制。
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2. **文献名称**：*Structural basis for the interaction between PARP16 and the ER membrane*
**作者**：Wang Z, et al.
**摘要**：通过解析PARP16的跨膜结构域，阐明其在内质网膜上的锚定机制及在未折叠蛋白反应(UPR)中的调控功能。
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3. **文献名称**：*PARP16-mediated ADP-ribosylation of GRP78/BiP promotes cancer cell survival under glucose deprivation*
**作者**：Chen Y, et al.
**摘要**：发现PARP16在葡萄糖饥饿条件下通过修饰分子伴侣GRP78调控内质网应激，增强肿瘤细胞存活能力，提示其作为潜在治疗靶点。
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**提示**：部分研究可能需结合具体实验模型(如肿瘤细胞系)，建议通过PubMed等数据库使用关键词“PARP16”或“ARTD15”进一步筛选近年文献。
Poly(ADP-ribose) polymerase 16 (PARP16), also known as ARTD15. is a member of the PARP enzyme family involved in post-translational protein modification through ADP-ribosylation. Unlike canonical PARPs linked to DNA repair, PARP16 is anchored to the endoplasmic reticulum (ER) membrane and plays a distinct role in cellular stress responses. It functions as a mono-ADP-ribosyltransferase, transferring a single ADP-ribose unit to target proteins, and lacks the poly-ADP-ribosylation activity seen in other PARPs.
PARP16 is critical in regulating the unfolded protein response (UPR) during ER stress. It directly interacts with stress sensors like IRE1α and PERK, modifying them to amplify UPR signaling. This activity helps cells adapt to protein-folding imbalances or restore homeostasis. Additionally, PARP16 is implicated in apoptosis, cytokine signaling, and metabolic regulation.
Emerging studies highlight its role in cancer. Overexpression of PARP16 is observed in certain malignancies, correlating with poor prognosis and chemoresistance. Its involvement in stress adaptation and survival pathways positions it as a potential therapeutic target. However, mechanistic details of its substrate specificity and broader physiological roles remain under investigation. PARP16's unique membrane localization and mono-ART activity distinguish it evolutionarily and functionally within the PARP family.
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