| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TRIM69 |
| Uniprot No | Q86WT6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-341aa |
| 氨基酸序列 | MEEELAIQQGQLETTLKELQTLRNMQKEAIAAHKENKLHLQQHVSMEFLKLHQFLHSKEKDILTELREEGKALNEEMELNLSQLQEQCLLAKDMLVSIQAKTEQQNSFDFLKDITTLLHSLEQGMKVLATRELISRKLNLGQYKGPIQYMVWREMQDTLCPGLSPLTLDPKTAHPNLVLSKSQTSVWHGDIKKIMPDDPERFDSSVAVLGSRGFTSGKWYWEVEVAKKTKWTVGVVRESIIRKGSCPLTPEQGFWLLRLRNQTDLKALDLPSFSLTLTNNLDKVGIYLDYEGGQLSFYNAKTMTHIYTFSNTFMEKLYPYFCPCLNDGGENKEPLHILHPQ |
| 预测分子量 | 66.3 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3篇关于TRIM69重组蛋白的虚构参考文献示例(基于学术文献常见结构模拟)：
1. **标题**：TRIM69重组蛋白的体外抗病毒活性及机制研究
**作者**：Zhang, Y. et al.
**摘要**：本研究通过原核表达系统纯化TRIM69重组蛋白，发现其能显著抑制甲型流感病毒复制。实验表明TRIM69通过泛素化修饰病毒核蛋白NP，促进其蛋白酶体降解，揭示了其新型抗病毒机制。
2. **标题**：TRIM69的晶体结构解析及其E3泛素连接酶活性位点鉴定
**作者**：Wang, L. et al.
**摘要**：利用X射线衍射技术首次解析了人源TRIM69蛋白的RING结构域晶体结构(分辨率2.1Å)，通过点突变实验证实Cys15/His18残基对E3泛素连接酶活性至关重要，为靶向药物设计提供结构基础。
3. **标题**：TRIM69重组蛋白在肝癌细胞凋亡调控中的双重作用
**作者**：Smith, J.R. et al.
**摘要**：研究发现TRIM69重组蛋白在HepG2细胞中呈现浓度依赖性促凋亡/抗凋亡双效作用。蛋白质组学分析显示其通过动态调控p53-MDM2泛素化平衡实现细胞命运决定，提示其在癌症治疗中的潜在价值。
注：以上为模拟文献，实际研究中请通过PubMed、Web of Science等数据库检索真实文献(检索词：TRIM69 recombinant protein)。如需真实文献线索，可重点关注近年《Nature Communications》《Cell Reports》等期刊关于TRIM蛋白家族的研究。
TRIM69 (Tripartite Motif-containing protein 69) is a member of the TRIM protein family, characterized by a conserved N-terminal tripartite motif comprising a RING domain, one or two B-box domains, and a coiled-coil region. These proteins are broadly implicated in cellular processes such as innate immunity, apoptosis, and antiviral defense. TRIM69. specifically, has garnered attention for its role in modulating immune signaling pathways and its potential involvement in host-pathogen interactions. The protein is encoded by the TRIM69 gene, located on human chromosome 11. and is expressed in various tissues, though its function remains less characterized compared to other TRIM family members.
Recombinant TRIM69 protein is engineered for in vitro studies to elucidate its structural and functional properties. Its RING domain, which confers E3 ubiquitin ligase activity, suggests a role in post-translational protein modification, potentially regulating protein degradation or signal transduction. The coiled-coil domain facilitates homo- or hetero-oligomerization, critical for forming functional complexes. Emerging research highlights TRIM69’s interaction with viral proteins, such as HIV-1 capsid, where it may act as a restriction factor by promoting viral protein degradation via ubiquitination. Additionally, studies link TRIM69 to the regulation of apoptosis and inflammasome activation, though mechanistic details are still under investigation.
The production of recombinant TRIM69 typically involves heterologous expression systems (e.g., E. coli, mammalian cells) to obtain soluble, active protein for biochemical assays, structural studies, or interaction mapping. Its applications span antiviral drug discovery, immune pathway analysis, and exploring its dual roles in tumor suppression and oncogenesis. Despite progress, unanswered questions persist regarding its tissue-specific functions, regulatory mechanisms, and potential therapeutic targeting. Further characterization of TRIM69 could uncover novel strategies for treating viral infections, autoimmune disorders, or cancers.
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