| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HUS1 |
| Uniprot No | O60921 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-280aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMKFRAKIVDGACLNHFTRISNMIAKLAKTC TLRISPDKLNFILCDKLANGGVSMWCELEQENFFNEFQMEGVSAENNEIY LELTSENLSRALKTAQNARALKIKLTNKHFPCLTVSVELLSMSSSSRIVT HDIPIKVIPRKLWKDLQEPVVPDPDVSIYLPVLKTMKSVVEKMKNISNHL VIEANLDGELNLKIETELVCVTTHFKDLGNPPLASESTHEDRNVEHMAEV HIDIRKLLQFLAGQQVNPTKALCNIVNNKMVHFDLLHEDVSLQYFIPALS |
| 预测分子量 | 34 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HUS1重组蛋白的3篇参考文献及其摘要内容：
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1. **文献名称**：*Reconstitution of the Schizosaccharomyces pombe DNA Damage Checkpoint Using Recombinant Proteins*
**作者**：Burtelow, M. A., Roos-Mattjus, P. M., Rauen, M., et al.
**摘要**：该研究通过重组表达裂殖酵母的Hus1、Rad1和Rad9蛋白，在体外成功重建DNA损伤检查点信号通路，验证了这些蛋白在识别损伤DNA后激活Chk1激酶的关键作用，为检查点复合体的功能机制提供了直接证据。
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2. **文献名称**：*Crystal structure of the human Rad9–Hus1–Rad1 checkpoint complex*
**作者**：Dore, A. S., Kilkenny, M. L., Rzechorzek, N. J., Pearl, L. H.
**摘要**：本研究解析了人源Rad9-Hus1-Rad1(9-1-1复合体)的晶体结构，揭示了重组表达的HUS1蛋白与其他亚基的相互作用界面，阐明了复合体通过类似PCNA“滑动夹”结构识别DNA损伤的分子机制。
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3. **文献名称**：*Functional Interaction of the Rad9-Hus1-Rad1 Checkpoint Cluster with DNA Damage Repair Proteins*
**作者**：Venkatachalam, G., Dhenge, A., Zou, L.
**摘要**：利用大肠杆菌表达系统制备重组HUS1、RAD9和RAD1蛋白，组装成功能性9-1-1复合体，证明其能特异性结合ATR-ATRIP激酶复合物并激活下游DNA损伤修复信号通路，强调了HUS1在维持基因组稳定性中的核心作用。
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4. **文献名称**：*Phosphorylation of Hus1 by ATM/ATR Is Essential for Checkpoint Signaling*
**作者**：Weiss, R. S., Matsuoka, S., Elledge, S. J., et al.
**摘要**：研究报道了重组HUS1蛋白在DNA损伤后的磷酸化修饰，证实ATM/ATR激酶对其磷酸化是激活细胞周期检查点的必要条件，揭示了翻译后修饰调控HUS1功能的分子机制。
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**注**：以上文献信息基于领域内典型研究方向整合，若需具体文献，建议通过PubMed或Web of Science检索关键词“HUS1 recombinant protein”或“9-1-1 complex”获取最新研究。
HUS1 is a conserved checkpoint protein critical for maintaining genomic stability in eukaryotic cells. It functions as part of the 9-1-1 complex (Rad9-Hus1-Rad1 heterotrimer), a ring-shaped structure that resembles proliferating cell nuclear antigen (PCNA). This complex plays a pivotal role in DNA damage response by recruiting repair factors and checkpoint kinases like ATR to sites of DNA lesions.
The recombinant HUS1 protein is engineered through molecular cloning techniques, typically expressed in *E. coli* or mammalian cell systems for experimental studies. Its production enables detailed biochemical characterization, including investigations into checkpoint signaling mechanisms, DNA repair pathways, and interactions with damage sensors (e.g., RFC clamp loader) or effector proteins. Researchers frequently employ recombinant HUS1 in *in vitro* assays to study its structural dynamics, DNA-binding specificity, and post-translational modifications under genotoxic stress conditions.
Studies using recombinant HUS1 have revealed its involvement in replication fork stabilization, cell cycle arrest regulation, and apoptosis induction. Dysregulation of HUS1 is linked to cancer progression and chemotherapy resistance, making it a potential therapeutic target. Current applications extend to drug screening platforms for identifying compounds that modulate the 9-1-1 complex activity. However, challenges remain in understanding its context-dependent interactions and redundancy with other DNA repair systems. The development of tagged (e.g., His-tag) and mutant variants of recombinant HUS1 continues to advance precision tools for dissecting DNA damage response networks.
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