| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DCP2 |
| Uniprot No | Q8IU60 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-385aa |
| 氨基酸序列 | METKRVEIPGSVLDDLCSRFILHIPSEERDNAIRVCFQIELAHWFYLDFY MQNTPGLPQCGIRDFAKAVFSHCPFLLPQGEDVEKVLDEWKEYKMGVPTY GAIILDETLENVLLVQGYLAKSGWGFPKGKVNKEEAPHDCAAREVFEETG FDIKDYICKDDYIELRINDQLARLYIIPGIPKDTKFNPKTRREIRNIEWF SIEKLPCHRNDMTPKSKLGLAPNKFFMAIPFIRPLRDWLSRRFGDSSDSD NGFSSTGSTPAKPTVEKLSRTKFRHSQQLFPDGSPGDQWVKHRQPLQQKP YNNHSEMSDLLKGKKCEKKLHPRKLQDNFETDAVYDLPSSSEDQLLEHAE GQPVACNGHCKFPFSSRAFLSFKFDHNAIMKILDL |
| 预测分子量 | 68 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DCP2重组蛋白的3篇参考文献示例(注：文献为假设性概括，实际研究中请以具体论文为准)：
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1. **标题**: *"Recombinant DCP2 Protein Exhibits Decapping Activity in vitro: Functional Characterization of the Human mRNA Decapping Enzyme"*
**作者**: Smith A, et al.
**摘要**: 本研究通过在大肠杆菌中表达并纯化重组人源DCP2蛋白，证明其具有特异性mRNA脱帽酶活性。体外实验表明，DCP2与辅助因子DCP1结合后可显著增强其水解mRNA 5'端帽子结构的能力，揭示了其在mRNA降解通路中的核心作用。
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2. **标题**: *"Structural Insights into DCP2 Recruitment by the LSM Complex in mRNA Decay"*
**作者**: Jones B, et al.
**摘要**: 通过X射线晶体学解析了重组DCP2蛋白与LSM复合物的结合结构，发现DCP2的N端结构域直接与LSM1-7环状复合物互作，阐明了脱帽酶在细胞质加工小体(P-body)中靶向mRNA的分子机制。
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3. **标题**: *"Regulation of Recombinant DCP2 Activity by Post-Translational Modifications in Cancer Cells"*
**作者**: Chen L, et al.
**摘要**: 研究利用昆虫细胞表达系统获得高纯度重组DCP2蛋白，发现其在肿瘤细胞中受磷酸化修饰(如AKT激酶介导的Ser237位点)调控，修饰后脱帽酶活性降低，导致特定致癌mRNA稳定性增加，促进癌细胞增殖。
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(注：以上文献为示例，实际引用需以真实发表的论文为准。)
**Background of DCP2 Recombinant Protein**
DCP2 (Decapping Enzyme 2) is a critical RNA-binding protein involved in mRNA metabolism, particularly in the removal of the 5' cap structure, a key step in eukaryotic mRNA decay. As a member of the Nudix hydrolase family, DCP2 catalyzes the hydrolysis of the m7GpppN cap, releasing m7GDP and uncapped mRNA, which is then rapidly degraded by exonucleases. This decapping process is tightly regulated and serves as a pivotal control point in post-transcriptional gene expression, influencing cellular responses to stress, development, and disease.
The recombinant DCP2 protein is engineered to study its enzymatic activity, structure, and interactions in vitro. Typically expressed in systems like *E. coli* or mammalian cells, the purified protein retains conserved functional domains, including the catalytic Nudix motif and regulatory regions that mediate interactions with co-factors such as DCP1. Edc4. and the LSM1-7 complex. These partnerships are essential for forming the active decapping complex, which integrates signals from mRNA surveillance pathways (e.g., nonsense-mediated decay).
Research using recombinant DCP2 has elucidated its role in cellular homeostasis and disease. Dysregulation of DCP2 is linked to neurological disorders, viral infections, and cancer, where aberrant mRNA turnover impacts cell proliferation or survival. For instance, reduced DCP2 activity correlates with stabilized oncogenic transcripts in certain cancers, highlighting its potential as a therapeutic target. Structural studies using recombinant proteins have also revealed mechanisms of catalysis and inhibition, aiding in drug discovery.
In summary, DCP2 recombinant protein serves as a vital tool for dissecting mRNA decay pathways and exploring interventions in diseases driven by disrupted RNA dynamics. Its study bridges molecular biology and translational research, offering insights into RNA-based regulation.
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