| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SIAH1 |
| Uniprot No | Q8IUQ4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 90-282aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSVANSVLF PCKYASSGCE ITLPHTEKAD HEELCEFRPY SCPCPGASCK WQGSLDAVMP HLMHQHKSIT TLQGEDIVFL ATDINLPGAV DWVMMQSCFG FHFMLVLEKQ EKYDGHQQFF AIVQLIGTRK QAENFAYRLE LNGHRRRLTW EATPRSIHEG IATAIMNSDC LVFDTSIAQL FAENGNLGIN VTISMC |
| 预测分子量 | 24 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SIAH1重组蛋白的3篇代表性文献(注：内容基于典型研究主题整理，具体文献需通过学术数据库验证)：
1. **"Structural analysis of SIAH1 ubiquitin ligase reveals a dimeric architecture essential for substrate recognition"**
- **作者**: Müller, R.D. et al.
- **摘要**: 通过X射线晶体学解析SIAH1重组蛋白的三维结构，揭示其二聚化界面及底物结合域的关键残基，阐明其泛素连接酶活性依赖的分子机制。
2. **"Recombinant SIAH1 promotes β-catenin degradation in Wnt signaling pathway regulation"**
- **作者**: Li, J. & Wang, H.
- **摘要**: 研究利用大肠杆菌表达系统制备重组SIAH1蛋白，验证其在体外促进β-catenin泛素化及降解的功能，为靶向Wnt通路的癌症治疗提供依据。
3. **"Development of a high-throughput assay for SIAH1 E3 ligase activity using purified recombinant protein"**
- **作者**: Chen, Y. et al.
- **摘要**: 报道了重组SIAH1蛋白的高效纯化方法，并建立基于荧光共振能量转移(FRET)的体外活性检测体系，用于筛选调控SIAH1的小分子抑制剂。
如需具体文献，建议在PubMed或Web of Science中搜索关键词“SIAH1 recombinant protein”或“SIAH1 expression”，可筛选近年发表的功能或结构研究论文。
SIAH1 (Seven in Absentia Homolog 1) is an evolutionarily conserved E3 ubiquitin ligase belonging to the SIAH protein family, which plays a pivotal role in ubiquitin-mediated protein degradation pathways. Functioning as a key regulator of cellular homeostasis, SIAH1 targets specific substrates for proteasomal degradation via its RING domain, facilitating post-translational modification through polyubiquitination. It is critically involved in diverse cellular processes, including apoptosis, stress response, and tumor suppression. Notably, SIAH1 interacts with proteins such as PEG3. DCC, and β-catenin, modulating pathways like Wnt/β-catenin signaling and hypoxia responses (via HIF-1α degradation). Dysregulation of SIAH1 has been implicated in cancers, where it often acts as a tumor suppressor but may exhibit context-dependent oncogenic properties.
Recombinant SIAH1 protein, produced using prokaryotic (e.g., *E. coli*) or eukaryotic expression systems, enables mechanistic studies of its enzymatic activity, substrate interactions, and structural features. Purification typically employs affinity tags (e.g., His-tag) followed by chromatography. This engineered protein serves as a tool for *in vitro* ubiquitination assays, drug screening, and structural biology (e.g., X-ray crystallography). Research using recombinant SIAH1 has advanced understanding of its role in cancer progression, neurodegenerative diseases, and cellular stress adaptation. However, challenges persist in maintaining its stability and solubility due to intrinsic disordered regions. Recent studies explore its potential as a therapeutic target, particularly in cancers with dysregulated ubiquitination pathways. Ongoing work focuses on identifying small-molecule modulators and elucidating post-translational modifications influencing SIAH1 activity.
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