| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RPAIN |
| Uniprot No | Q86UA6-6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-106aa |
| 氨基酸序列 | GSSHHHHHH SSGLVPRGSH MGSMAESLRS PRRSLYKLVG SPPWKEAFRQ RCLERMRNSR DRLLNRYRQA GSSGPGNSQN SFLVQEVMEE EWNALQSVEN CPEDLAQLEE LIDMAVLEEI QQELINQGL |
| 预测分子量 | 15 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RPAIN重组蛋白的假设性参考文献示例(请注意，这些文献为虚构示例，仅供参考格式)：
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1. **文献名称**: *"Expression and Functional Analysis of Recombinant RPAIN in DNA Repair Pathways"*
**作者**: Smith, J. et al. (2015)
**摘要**: 本研究在大肠杆菌中成功表达并纯化了重组RPAIN蛋白，证实其与复制蛋白A(RPA)的相互作用。通过体外实验发现，重组RPAIN能够增强RPA复合物在单链DNA上的稳定性，提示其在DNA损伤修复中的潜在作用。
2. **文献名称**: *"Structural Insights into RPAIN's Role in Homologous Recombination"*
**作者**: Lee, S. & Kim, M. (2020)
**摘要**: 利用X射线晶体学解析了重组RPAIN蛋白的三维结构，揭示了其N端结构域与RPA70亚基的关键结合位点。实验表明，重组RPAIN通过调控RPA构象变化促进同源重组修复效率。
3. **文献名称**: *"RPAIN Overexpression Enhances Cancer Cell Proliferation via DNA Repair Modulation"*
**作者**: Zhang, Y. et al. (2022)
**摘要**: 通过体外表达重组RPAIN蛋白，研究发现其在多种癌细胞系中过表达可加速DNA损伤修复并促进细胞增殖，提示RPAIN可能作为癌症治疗的潜在靶点。
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**注意**：以上文献为假设性示例，实际研究中请通过学术数据库(如PubMed、Web of Science)检索真实文献。若需进一步协助，请提供更具体的蛋白背景或研究领域。
**Background of RPAIN Recombinant Protein**
RPAIN (RPA-interacting protein), also known as hCINAP or AKTIP, is a multifunctional protein involved in critical cellular processes, including DNA repair, cell cycle regulation, and ubiquitination. It interacts directly with Replication Protein A (RPA), a single-stranded DNA-binding complex essential for DNA replication, recombination, and repair. This interaction positions RPAIN as a regulatory player in the DNA damage response, particularly in coordinating RPA’s role during replication stress or genotoxic events.
Structurally, RPAIN contains an acidic domain and a C-terminal region that mediates binding to RPA. Beyond DNA repair, RPAIN functions as an adaptor for the E3 ubiquitin ligase CHFR, promoting the ubiquitination and degradation of target proteins, thereby influencing cell cycle checkpoints and apoptosis. Its involvement in the ubiquitin-proteasome system highlights its regulatory importance in protein turnover and cellular homeostasis.
Recombinant RPAIN protein is engineered using expression systems (e.g., *E. coli* or mammalian cells*) to produce purified, functional protein for research. Its recombinant form enables studies on molecular mechanisms underlying DNA damage responses, cancer biology (e.g., RPAIN dysregulation in tumors), and neurodegenerative diseases linked to proteostatic dysfunction. Researchers also utilize it to explore RPAIN’s structural interactions with RPA or other partners via techniques like co-immunoprecipitation or crystallography.
Overall, RPAIN recombinant protein serves as a vital tool for dissecting its dual roles in genome stability and protein degradation, offering insights into therapeutic strategies for cancer and diseases associated with DNA repair or ubiquitination pathways.
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