| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TRIM54 |
| Uniprot No | Q9BYV2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-358 aa |
| 活性数据 | MNFTVGFKPL LGDAHSMDNL EKQLICPICL EMFSKPVVIL PCQHNLCRKC ANDVFQASNP LWQSRGSTTV SSGGRFRCPS CRHEVVLDRH GVYGLQRNLL VENIIDIYKQ ESSRPLHSKA EQHLMCEEHE EEKINIYCLS CEVPTCSLCK VFGAHKDCEV APLPTIYKRQ KSELSDGIAM LVAGNDRVQA VITQMEEVCQ TIEDNSRRQK QLLNQRFESL CAVLEERKGE LLQALAREQE EKLQRVRGLI RQYGDHLEAS SKLVESAIQS MEEPQMALYL QQAKELINKV GAMSKVELAG RPEPGYESME QFTVRVEHVA EMLRTIDFQP GASGEEEEVA PDGEEGSAGP EEERPDGP |
| 分子量 | 40.3 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. |
以下是关于TRIM54蛋白的3篇研究文献的简要总结(注：以下为模拟构造的文献示例，实际文献需通过学术数据库核实)：
1. **标题**：*TRIM54 regulates skeletal muscle differentiation through ubiquitination of Akt*
**作者**：Smith A, et al.
**摘要**：该研究发现TRIM54通过泛素化修饰Akt蛋白，调控哺乳动物骨骼肌细胞的分化过程，缺失TRIM54会抑制成肌细胞的融合及肌管形成，提示其在肌肉发育中的关键作用。
2. **标题**：*TRIM54 promotes hepatocellular carcinoma progression by activating Wnt/β-catenin signaling*
**作者**：Zhang Y, et al.
**摘要**：研究揭示TRIM54在肝癌组织中高表达，通过结合并稳定β-catenin蛋白，激活Wnt信号通路，促进肿瘤细胞增殖和转移，提示其作为肝癌潜在治疗靶点。
3. **标题**：*Structural insights into TRIM54 RING domain mediating E3 ligase activity*
**作者**：Brown CJ, et al.
**摘要**：本文解析了TRIM54蛋白RING结构域的晶体结构，阐明其与E2结合并催化泛素转移的分子机制，为设计靶向TRIM54的小分子抑制剂提供结构基础。
建议通过**PubMed**或**Web of Science**检索实际文献，输入关键词“TRIM54”或“Tripartite motif-containing protein 54”获取最新研究。
TRIM54. a member of the tripartite motif (TRIM) protein family, is characterized by its conserved RING finger, B-box, and coiled-coil domains. Predominantly expressed in skeletal and cardiac muscle tissues, it plays a critical role in cytoskeletal organization, myoblast differentiation, and muscle development. TRIM54 interacts with microtubules and associated proteins, regulating their dynamics and stability through its E3 ubiquitin ligase activity, which facilitates substrate ubiquitination and degradation via the proteasome. Studies highlight its involvement in maintaining sarcomere integrity and muscle cell architecture, with knockout models showing defects in muscle regeneration and sarcomere assembly. Dysregulation of TRIM54 is linked to muscular dystrophies, cardiomyopathies, and certain cancers, suggesting broader roles in cellular homeostasis and disease. Its dual function in structural regulation and ubiquitin-mediated signaling positions TRIM54 as a key molecular mediator in health and pathology, though precise mechanisms remain under investigation. Current research aims to elucidate its interactome, tissue-specific functions, and therapeutic potential in muscle-related disorders.
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