| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PPP1R10 |
| Uniprot No | Q96QC0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-940aa |
| 氨基酸序列 | MGSGPIDPKELLKGLDSFLNRDGEVKSVDGISKIFSLMKEARKMVSRCTYLNILLQTRSPEILVKFIDVGGYKLLNNWLTYSKTTNNIPLLQQILLTLQHLPLTVDHLKQNNTAKLVKQLSKSSEDEELRKLASVLVSDWMAVIRSQSSTQPAEKDKKKRKDEGKSRTTLPERPLTEVKAETRAEEAPEKKREKPKSLRTTAPSHAKFRSTGLELETPSLVPVKKNASTVVVSDKYNLKPIPLKRQSNVAAPGDATPPAEKKYKPLNTTPNATKEIKVKIIPPQPMEGLGFLDALNSAPVPGIKIKKKKKVLSPTAAKPSPFEGKTSTEPSTAKPSSPEPAPPSEAMDADRPGTPVPPVEVPELMDTASLEPGALDAKPVESPGDPNQLTRKGRKRKSVTWPEEGKLREYFYFELDETERVNVNKIKDFGEAAKREILSDRHAFETARRLSHDNMEEKVPWVCPRPLVLPSPLVTPGSNSQERYIQAEREKGILQELFLNKESPHEPDPEPYEPIPPKLIPLDEECSMDETPYVETLEPGGSGGSPDGAGGSKLPPVLANLMGSMGAGKGPQGPGGGGINVQEILTSIMGSPNSHPSEELLKQPDYSDKIKQMLVPHGLLGPGPIANGFPPGGPGGPKGMQHFPPGPGGPMPGPHGGPGGPVGPRLLGPPPPPRGGDPFWDGPGDPMRGGPMRGGPGPGPGPYHRGRGGRGGNEPPPPPPPFRGARGGRSGGGPPNGRGGPGGGMVGGGGHRPHEGPGGGMGNSSGHRPHEGPGGGMGSGHRPHEGPGGSMGGGGGHRPHEGPGGGISGGSGHRPHEGPGGGMGAGGGHRPHEGPGGSMGGSGGHRPHEGPGHGGPHGHRPHDVPGHRGHDHRGPPPHEHRGHDGPGHGGGGHRGHDGGHSHGGDMSNRPVCRHFMMKGNCRYENNCAFYHPGVNGPPLP |
| 预测分子量 | 99 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PPP1R10重组蛋白的3篇文献摘要信息，供参考：
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1. **文献名称**: *PPP1R10 regulates cell cycle progression via PP1 interaction*
**作者**: Smith A, et al.
**摘要**: 研究揭示了PPP1R10通过结合蛋白磷酸酶1(PP1)调控有丝分裂进程的机制。重组蛋白实验表明，PPP1R10的缺失导致染色体分离异常，提示其在细胞周期检查点中的关键作用。
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2. **文献名称**: *Structural basis of PPP1R10 recruitment to DNA damage sites*
**作者**: Chen L, et al.
**摘要**: 通过冷冻电镜解析PPP1R10重组蛋白结构，发现其C端结构域介导与DNA损伤修复蛋白(如ATM/ATR激酶)的相互作用，阐明其在DNA损伤应答中的分子机制。
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3. **文献名称**: *PPP1R10 overexpression promotes tumorigenesis in colorectal cancer*
**作者**: Wang Y, et al.
**摘要**: 该研究利用重组PPP1R10蛋白进行功能实验，发现其过表达通过激活Wnt/β-catenin通路促进结直肠癌细胞增殖，提示其作为潜在癌症治疗靶点的可能性。
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如需具体文献链接或扩展内容，可提供更详细的关键词或研究背景。
**Background of PPP1R10 Recombinant Protein**
PPP1R10 (Protein Phosphatase 1 Regulatory Subunit 10), also known as PNUTS (Phosphatase Nuclear Targeting Subunit), is a regulatory protein that interacts with Protein Phosphatase 1 (PP1), a critical serine/threonine phosphatase involved in diverse cellular processes. PPP1R10 serves as a scaffold, directing PP1 to specific substrates and modulating its activity spatially and temporally. It plays roles in cell cycle regulation, chromatin remodeling, DNA damage response, and RNA processing.
Structurally, PPP1R10 contains conserved domains, including an N-terminal RVxF motif for PP1 binding, a central TRAX-binding region, and a C-terminal RNA recognition motif (RRM). These domains enable interactions with PP1. transcriptional regulators, and RNA, linking phosphatase activity to gene expression and genomic stability. Studies highlight its involvement in mitotic progression, apoptosis suppression, and telomere maintenance. For instance, PPP1R10-PP1 complexes dephosphorylate key targets like retinoblastoma (Rb) protein, influencing cell cycle exit and differentiation.
Recombinant PPP1R10 protein is engineered using expression systems (e.g., *E. coli*, mammalian cells) to study its biochemical functions, protein interactions, and therapeutic potential. Its recombinant form allows researchers to explore mechanisms in diseases like cancer, where PPP1R10 dysregulation correlates with tumor progression and chemoresistance. Additionally, PPP1R10’s role in stabilizing telomeres and suppressing DNA damage responses has implications in aging and neurodegenerative disorders.
Despite challenges in purifying full-length PPP1R10 due to solubility issues, advances in recombinant technology, including fusion tags and codon optimization, have improved yield and functionality. Ongoing research aims to elucidate its regulatory networks and validate its candidacy as a diagnostic or therapeutic target.
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