| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TRIM74 |
| Uniprot No | Q86UV6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-250 aa |
| 活性数据 | MAWQVSLLEL EDWLQCPICL EVFKESLMLQ CGHSYCKGCL VSLSYHLDTK VRCPMCWQVV DGSSSLPNVS LAWVIEALRL PGDPEPKVCV HHRNPLSLFC EKDQELICGL CGLLGSHQHH PVTPVSTVCS RMKEELAALF SELKQEQKKV DELIAKLVKN RTRIVNESDV FSWVIRREFQ ELRHPVDEEK ARCLEGIGGH TRGLVASLDM QLEQAQGTRE RLAQAECVLE QFGNEDHHEF IWKFHSMASR |
| 分子量 | 28.5 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TRIM74蛋白的3篇示例参考文献(注：内容为模拟虚构，实际文献需查阅数据库确认)：
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1. **文献名称**：*TRIM74 Acts as a Viral Restriction Factor by Promoting Ubiquitination of Hepatitis B Virus Core Protein*
**作者**：Chen L, Wang Y, et al.
**摘要**：本研究揭示TRIM74通过其E3泛素连接酶活性靶向乙肝病毒核心蛋白，诱导其泛素化降解，抑制病毒组装，并激活Ⅰ型干扰素信号通路增强先天免疫应答。
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2. **文献名称**：*Overexpression of TRIM74 in Non-Small Cell Lung Cancer Correlates with Poor Prognosis*
**作者**：Zhang R, Liu X, et al.
**摘要**：通过临床样本分析，发现TRIM74在非小细胞肺癌组织中显著高表达，并通过调控PI3K/AKT/mTOR通路促进肿瘤细胞迁移和侵袭，提示其作为潜在治疗靶点的可能性。
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3. **文献名称**：*Structural Insights into the Multimerization and Substrate Recognition of TRIM74*
**作者**：Tanaka K, Nakamura S, et al.
**摘要**：利用X射线晶体学解析了TRIM74的B-box和Coiled-coil结构域的三维结构，揭示了其形成同源多聚体的分子机制及底物结合的关键氨基酸位点。
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**备注**：以上文献信息为示例，实际研究中建议通过PubMed、Web of Science等平台以“TRIM74 protein”或“TRIM74 AND (function/structure/cancer)”为关键词检索最新文献。
**Background of TRIM74 Protein**
TRIM74 (Tripartite Motif-containing Protein 74) belongs to the TRIM family, characterized by a conserved tripartite motif comprising a RING domain, B-box zinc fingers, and a coiled-coil region. These domains often confer E3 ubiquitin ligase activity, enabling TRIM proteins to regulate diverse cellular processes like innate immunity, antiviral defense, and protein degradation via ubiquitination.
While many TRIM family members are well-studied, TRIM74 remains less understood. It is encoded by the *TRIM74* gene, located on human chromosome 7q33. Expression of TRIM74 has been detected in tissues such as testes, placenta, and immune cells, suggesting potential roles in reproduction or immunity. Recent studies hint at its involvement in modulating innate immune responses and interfering with viral replication pathways, though mechanistic details are sparse.
Interestingly, TRIM74 exhibits species-specific features. Unlike most TRIM proteins, it lacks a canonical PRY/SPRY domain, which typically mediates protein-protein interactions. This structural divergence implies unique functional adaptations. Dysregulation of TRIM74 has been loosely associated with cancers (e.g., hepatocellular carcinoma) and immune disorders, but conclusive evidence is lacking. Current research focuses on elucidating its substrate targets, post-translational modifications, and interplay with viral or cellular proteins. Further studies are needed to define its physiological and pathological relevance comprehensively.
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