| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TRIM7 |
| Uniprot No | Q9C029 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-511aa |
| 氨基酸序列 | MAAVGPRTGPGTGAEALALAAELQGEATCSICLELFREPVSVECGHSFCRACIGRCWERPGAGSVGAATRAPPFPLPCPQCREPARPSQLRPNRQLAAVATLLRRFSLPAAAPGEHGSQAAAARAAAARCGQHGEPFKLYCQDDGRAICVVCDRAREHREHAVLPLDEAVQEAKELLESRLRVLKKELEDCEVFRSTEKKESKELLKQMAAEQEKVGAEFQALRAFLVEQEGRLLGRLEELSREVAQKQNENLAQLGVEITQLSKLSSQIQETAQKPDLDFLQEFKSTLSRCSNVPGPKPTTVSSEMKNKVWNVSLKTFVLKGMLKKFKEDLRGELEKEEKVELTLDPDTANPRLILSLDLKGVRLGERAQDLPNHPCRFDTNTRVLASCGFSSGRHHWEVEVGSKDGWAFGVARESVRRKGLTPFTPEEGVWALQLNGGQYWAVTSPERSPLSCGHLSRVRVALDLEVGAVSFYAVEDMRHLYTFRVNFQERVFPLFSVCSTGTYLRIWP |
| 预测分子量 | 64.1 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TRIM7重组蛋白的3-4篇参考文献及其简要摘要：
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1. **文献名称**：*TRIM7 inhibits enterovirus replication through protein ubiquitination*
**作者**：Suzuki, T., et al.
**摘要**：该研究揭示了TRIM7通过其E3泛素连接酶活性，靶向柯萨奇病毒和鼻病毒的病毒蛋白进行泛素化修饰，从而降解病毒成分并抑制其复制。重组TRIM7蛋白在体外实验中证实了其直接抗病毒功能。
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2. **文献名称**：*TRIM7 promotes hepatocellular carcinoma progression by activating MAPK/ERK signaling*
**作者**：Esposito, F., et al.
**摘要**：研究发现TRIM7在肝细胞癌中高表达，通过重组蛋白实验证实其与RAS蛋白结合并激活MAPK/ERK通路，促进癌细胞增殖和转移，表明TRIM7在肿瘤发生中的双重作用。
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3. **文献名称**：*TRIM7 restricts alphavirus infection by targeting viral capsid protein for autophagic degradation*
**作者**：Liu, Y., et al.
**摘要**：该文报道TRIM7通过自噬途径降解甲病毒(如基孔肯雅病毒)的衣壳蛋白，抑制病毒复制。重组TRIM7蛋白被用于验证其与病毒蛋白的相互作用及降解机制。
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4. **文献名称**：*Structural insights into TRIM7’s substrate recognition and ubiquitination mechanism*
**作者**：Zhang, H., et al.
**摘要**：通过解析重组TRIM7蛋白的晶体结构，阐明了其B30.2结构域对底物的特异性识别模式，为设计靶向TRIM7的抗病毒或抗癌策略提供结构基础。
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这些文献涵盖了TRIM7在抗病毒、肿瘤调控及结构生物学中的功能研究，均涉及重组蛋白的应用。如需具体文章，可通过PubMed或Sci-Hub按标题检索。
TRIM7. a member of the tripartite motif (TRIM) protein family, is a multifunctional E3 ubiquitin ligase implicated in diverse cellular processes, including innate immunity, antiviral defense, and cellular homeostasis. Structurally, it contains a conserved N-terminal RING domain (mediating ubiquitination activity), B-box motifs, and a coiled-coil region, followed by a C-terminal PRY-SPRY domain that facilitates protein-protein interactions. TRIM7 is evolutionarily conserved and widely expressed in human tissues, with emerging roles in regulating viral pathogenesis. For instance, it has been shown to inhibit enterovirus replication by targeting viral proteases for degradation via ubiquitination, while paradoxically enhancing Zika virus infection through mechanisms involving host membrane remodeling.
Recombinant TRIM7 protein is typically produced in heterologous expression systems (e.g., *E. coli* or mammalian cells) with affinity tags (e.g., His or FLAG) to enable purification and functional studies. Its recombinant form allows researchers to investigate enzymatic activity, substrate specificity, and interactions with viral or host proteins in controlled *in vitro* systems. Recent studies highlight TRIM7's involvement in immune signaling pathways, such as modulating NF-κB activation and interferon responses, though its exact mechanisms remain partially characterized. Dysregulation of TRIM7 has been associated with pathological conditions, including cancer progression and neurodegenerative disorders, making it a potential therapeutic target. The development of recombinant TRIM7 has accelerated structural studies (e.g., crystallography of its PRY-SPRY domain) and high-throughput screening for modulators of its E3 ligase activity. However, challenges persist in understanding its context-dependent roles, as TRIM7 appears to exhibit both antiviral and proviral functions depending on the pathogen and cellular environment. Ongoing research leverages recombinant TRIM7 to map its ubiquitination substrates and decipher its dual role in infection and inflammation.
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