纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | PARP12 |
Uniprot No | Q9H0J9 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-701aa |
氨基酸序列 | MAQAGVVGEVTQVLCAAGGALELPELRRRLRMGLSADALERLLRQRGRFVVAVRAGGAAAAPERVVLAASPLRLCRAHQGSKPGCVGLCAQLHLCRFMVYGACKFLRAGKNCRNSHSLTTEHNLSVLRTHGVDHLSYNELCQLLFQNDPWLLPEICQHYNKGDGPHGSCAFQKQCIKLHICQYFLQGECKFGTSCKRSHDFSNSENLEKLEKLGMSSDLVSRLPTIYRNAHDIKNKSSAPSRVPPLFVPQGTSERKDSSGSVSPNTLSQEEGDQICLYHIRKSCSFQDKCHRVHFHLPYRWQFLDRGKWEDLDNMELIEEAYCNPKIERILCSESASTFHSHCLNFNAMTYGATQARRLSTASSVTKPPHFILTTDWIWYWSDEFGSWQEYGRQGTVHPVTTVSSSDVEKAYLAYCTPGSDGQAATLKFQAGKHNYELDFKAFVQKNLVYGTTKKVCRRPKYVSPQDVTTMQTCNTKFPGPKSIPDYWDSSALPDPGFQKITLSSSSEEYQKVWNLFNRTLPFYFVQKIERVQNLALWEVYQWQKGQMQKQNGGKAVDERQLFHGTSAIFVDAICQQNFDWRVCGVHGTSYGKGSYFARDAAYSHHYSKSDTQTHTMFLARVLVGEFVRGNASFVRPPAKEGWSNAFYDSCVNSVSDPSIFVIFEKHQVYPEYVIQYTTSSKPSVTPSILLALGSLFSSRQ |
预测分子量 | 86.5 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PARP12重组蛋白的3篇示例文献(注:文献为假设性示例,仅供参考):
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1. **文献名称**:*PARP12 mediates antiviral innate immunity through RNA interaction and ADP-ribosylation*
**作者**:Atkins et al. (2018)
**摘要**:研究利用重组PARP12蛋白,揭示了其在抗病毒先天免疫中的作用。实验表明,PARP12通过N端RNA结合结构域识别病毒RNA,并通过C端催化结构域介导ADP-核糖基化修饰宿主蛋白,抑制病毒复制。
2. **文献名称**:*Structural insights into the catalytic mechanism of PARP12*
**作者**:Smith et al. (2020)
**摘要**:通过表达并纯化PARP12重组蛋白的催化结构域,结合X射线晶体学分析,揭示了其ADP-核糖基转移酶活性依赖的关键氨基酸残基,为设计PARP12特异性抑制剂提供了结构基础。
3. **文献名称**:*PARP12 regulates endoplasmic reticulum stress via ADP-ribosylation of GRP78*
**作者**:Lee et al. (2021)
**摘要**:研究利用哺乳动物细胞表达系统获得重组PARP12蛋白,证明其在内质网应激中通过修饰分子伴侣GRP78调控未折叠蛋白反应(UPR),影响细胞存活与凋亡平衡。
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**说明**:若需真实文献,建议在PubMed或Web of Science中检索关键词“PARP12 recombinant”“PARP12 function”等,并筛选涉及重组蛋白表达、功能或机制的研究。
PARP12 (Poly(ADP-ribose) polymerase 12) is a member of the PARP protein family, which is characterized by its conserved catalytic domain responsible for transferring ADP-ribose units to target proteins. As part of the larger ARTD (ADP-ribosyltransferase diphtheria toxin-like) subfamily, PARP12 plays roles in diverse cellular processes, including stress response, RNA metabolism, and antiviral defense. Unlike classical PARPs involved in DNA repair (e.g., PARP1/2), PARP12 is classified as a "mono-ARTD" due to its predominant mono-ADP-ribosyltransferase activity. It contains multiple functional domains, such as RNA-binding WWE domains and a C-terminal catalytic domain, enabling interactions with nucleic acids and proteins.
Recombinant PARP12 protein is engineered for in vitro studies to dissect its enzymatic mechanisms, substrate specificity, and biological functions. Produced typically in bacterial or mammalian expression systems, the purified protein retains catalytic activity and structural integrity, allowing researchers to explore its role in stress granule formation, RNA virus restriction, and post-translational modification pathways. PARP12 is implicated in modulating innate immunity by targeting viral replication machinery or host factors, as seen in studies on coronaviruses and flaviviruses. Its involvement in cellular stress adaptation also links it to pathologies like cancer and neurodegenerative diseases.
Recent interest in PARP12 stems from its potential as a therapeutic target, particularly in antiviral drug development. Recombinant PARP12 facilitates high-throughput screening for inhibitors or activators and structural studies to guide rational drug design. Additionally, its interaction with stress-responsive pathways highlights its regulatory role in maintaining proteostasis and RNA stability under oxidative or endoplasmic reticulum stress. Ongoing research aims to clarify its dual functions in promoting cell survival or death, depending on cellular context, underscoring its complexity in health and disease.
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