| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | SUS1 |
| Uniprot No | P31925 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-218aa |
| 氨基酸序列 | ARLDRVKNMTGPVEISGKKARLRELANPVIVAGDHGKESKDRDEAEEQGGFKKMYSLIDDYKFKGHIRLISAQMNRVRNGELYQYICDTKGAFVQPAYEAFRLDCDRVHEVRSAKDRDLPWRPCEIIADGVSGLHIDPYHSDKDADILVNFFDKCNADPSYWDEISQGGQRIYEKYTWKLYSERLMTLTGAYGFWNYVSKLERGDTRYIDMFYALEYP |
| 预测分子量 | 41.3 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. |
以下是模拟生成的关于SUS1重组蛋白的参考文献示例(实际文献可能需要通过学术数据库查询)：
1. **标题**：Functional Characterization of Recombinant SUS1 in mRNA Export and Histone Deacetylation
**作者**：Rodríguez-Navarro S, et al.
**摘要**：研究利用大肠杆菌系统重组表达酵母SUS1蛋白，证实其通过参与组蛋白H2B去乙酰化和mRNA输出复合体的组装，调控基因表达及核质运输过程。
2. **标题**：Structural Insights into the Role of Sus1 in the SAGA Complex
**作者**：Köhler A, et al.
**摘要**：通过X射线晶体学解析重组SUS1蛋白结构，揭示其与SAGA复合体中Ubp8的相互作用机制，阐明其在染色质修饰中的结构基础。
3. **标题**：Optimization of Recombinant SUS1 Expression in Pichia pastoris for Functional Studies
**作者**：Li H, et al.
**摘要**：报道在毕赤酵母中高效分泌表达SUS1重组蛋白的策略，纯化后的蛋白在体外验证了其促进mRNA-蛋白复合体形成的活性。
4. **标题**：SUS1 Recombinant Protein as a Novel Tool for Epigenetic Modification Analysis
**作者**：Wang Y, et al.
**摘要**：开发基于重组SUS1蛋白的体外组蛋白去乙酰化检测体系，证明其在表观遗传学研究中的应用潜力。
**注意**：以上文献信息为模拟生成，仅用于示例用途。建议通过PubMed、Web of Science或Google Scholar搜索关键词“SUS1 recombinant protein”或“SUS1 yeast complex”获取真实文献。
**Background of SUS1 Recombinant Protein**
SUS1. initially identified in yeast (*Saccharomyces cerevisiae*), is a conserved eukaryotic protein involved in mRNA export and histone H2B deubiquitination. It functions as a critical regulatory component in two distinct macromolecular complexes: the SAGA (Spt-Ada-Gcn5 acetyltransferase) complex, which modulates chromatin remodeling and transcriptional activation, and the TREX-2 complex, which facilitates mRNA export from the nucleus to the cytoplasm. This dual association underscores SUS1's role in coupling transcriptional elongation with nuclear mRNA transport, ensuring efficient gene expression.
The recombinant SUS1 protein is engineered using DNA cloning techniques, where the *SUS1* gene is expressed in heterologous systems like *E. coli* or yeast. Purification methods such as affinity chromatography yield highly enriched SUS1. enabling functional and structural studies. Research on SUS1 recombinant protein has provided insights into its molecular interactions, particularly its ability to bind ubiquitin-specific proteases (e.g., Ubp8 in SAGA) and export factors (e.g., Sac3 in TREX-2). Structural analyses, including X-ray crystallography and cryo-EM, have revealed conformational flexibility critical for its dual-complex functionality.
Studies using recombinant SUS1 have also explored its role in maintaining genomic stability and cellular stress responses. Dysregulation of SUS1-associated pathways is linked to diseases, including cancers and neurodegenerative disorders, highlighting its potential as a therapeutic target. Overall, SUS1 recombinant protein serves as a vital tool for dissecting mechanisms of gene expression regulation and nuclear transport in eukaryotes.
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