| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SUGT1 |
| Uniprot No | Q9Y2Z0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 115-365aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMHRVGQAGLQLLTSSDPPALDSQSAGITGA DANFSVWIKRCQEAQNGSESEVWTHQSKIKYDWYQTESQVVITLMIKNVQ KNDVNVEFSEKELSALVKLPSGEDYNLKLELLHPIIPEQSTFKVLSTKIE IKLKKPEAVRWEKLEGQGDVPTPKQFVADVKNLYPSSSPYTRNWDKLVGE IKEEEKNEKLEGDAALNRLFQQIYSDGSDEVKRAMNKSFMESGGTVLSTN WSDVGKRKVEINPPDDMEWKKY |
| 预测分子量 | 31 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SUGT1重组蛋白的3篇参考文献概览(注：文献为示例性质，实际内容需根据真实研究调整)：
1. **文献名称**: "Recombinant SUGT1 Expression and Its Role in HSP90 Chaperone Complex Assembly"
**作者**: Smith J, et al.
**摘要**: 研究通过大肠杆菌系统重组表达SUGT1蛋白，验证其与HSP90的相互作用，揭示其在分子伴侣复合体组装中的调控作用。
2. **文献名称**: "Structural Insights into SUGT1-Mediated Protein Quality Control"
**作者**: Lee S, et al.
**摘要**: 利用X射线晶体学解析重组人源SUGT1蛋白结构，阐明其TPR结构域结合错误折叠蛋白的分子机制，为靶向治疗提供依据。
3. **文献名称**: "Functional Characterization of Recombinant SUGT1 in Yeast Phenotypic Rescue"
**作者**: Tanaka K, et al.
**摘要**: 在酵母模型中异源表达重组SUGT1蛋白，证明其可恢复sgp1突变株的增殖缺陷，证实其进化保守的蛋白质量控制功能。
(提示：若需真实文献，建议通过PubMed或Sci-Hub检索关键词“SUGT1 recombinant”或“SUGT1 expression”获取最新研究。)
SUGT1 (SGT1 Homolog, MIS12 Kinetochore Complex Assembly Cochaperone) is a conserved eukaryotic protein that plays a critical role in maintaining cellular protein homeostasis and kinetochore assembly. Functioning as a co-chaperone, it interacts with heat shock proteins (e.g., HSP70/HSC70) to facilitate proper folding of client proteins and mitigate stress-induced proteotoxicity. SUGT1 contains tetratricopeptide repeat (TPR) domains that mediate protein-protein interactions, enabling its involvement in diverse pathways including cell cycle regulation, stress response, and quality control of mislocalized proteins.
Recombinant SUGT1 protein is engineered through heterologous expression systems (e.g., E. coli, mammalian cells) to study its structural and functional properties. This purified protein retains biological activity, allowing researchers to investigate its chaperone functions, ATPase regulation, and binding partners in vitro. Its recombinant form has become essential for crystallographic studies, revealing conformational changes during client protein recognition.
Research highlights SUGT1's dual roles: 1) In chromatin-associated protein surveillance, where it collaborates with the BAG6 complex to degrade mislocalized membrane proteins; 2) In kinetochore assembly through interactions with the MIS12 complex, crucial for chromosome segregation. Dysregulation of SUGT1 is implicated in cancer (via mitotic errors), neurodegenerative diseases (e.g., impaired clearance of aggregation-prone proteins), and viral infection mechanisms. Current studies leverage recombinant SUGT1 to develop targeted therapies modulating protein quality control pathways, with particular interest in HSP90-independent chaperone networks. Its conserved structure-function relationships across species make it a valuable model for evolutionary studies of stress adaptation mechanisms.
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