| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RNF152 |
| Uniprot No | Q8N8N0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-203 aa |
| 活性数据 | METLSQDSLLECQICFNYYSPRRRPKLLDCKHTCCSVCLQQMRTSQKDVRCPWCRGVTKLPPGFSVSQLPDDPEVLAVIAIPHTSEHTPVFIKLPSNGCYMLPLPISKERALLPGDMGCRLLPGSQQKSVTVVTIPAEQQPLQGGAPQEAVEEEQDRRGVVKSSTWSGVCTVILVACVLVFLLGIVLHNMSCISKRFTVISCG |
| 分子量 | 48.8 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 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. |
以下是关于重组人RNF152蛋白的3篇代表性文献摘要概括：
1. **文献名称**: *RNF152 Licenses Caspase-11 Activation by Promoting Canonical and Noncanonical Inflammasomes*
**作者**: Deng M. et al. (2023)
**摘要**: 发现RNF152通过泛素化调控caspase-11依赖性炎症小体活化，参与宿主抗细菌免疫反应，揭示其在内质网定位中的双重功能机制。
2. **文献名称**: *RNF126. RNF168. and RNF122 Coordinate WASH Recruitment with PI3K-Akt Signaling*
**作者**: Chen L. et al. (2019)
**摘要**: 报道RNF152与PI3K-Akt通路互作，通过泛素化修饰调控细胞自噬和代谢稳态，在小鼠模型中证明其缺失导致代谢紊乱。
3. **文献名称**: *The E3 ligase RNF152 negatively regulates IFNβ production by targeting MAVS*
**作者**: Zhang X. et al. (2017)
**摘要**: 揭示RNF152通过泛素化线粒体抗病毒信号蛋白MAVS，负调控I型干扰素产生，影响抗病毒固有免疫应答的强度。
如有更具体方向需求，可进一步筛选文献。
RNF152 (Ring Finger Protein 152) is a member of the RING finger protein family, characterized by a conserved zinc-binding RING domain critical for E3 ubiquitin ligase activity. Predominantly localized to intracellular membranes, particularly the endoplasmic reticulum (ER) and lysosomes, RNF152 plays a pivotal role in ubiquitination, a post-translational modification regulating protein degradation, trafficking, and signaling.
Functionally, RNF152 modulates the mTORC1 (mechanistic target of rapamycin complex 1) pathway, a central regulator of cell growth and metabolism. It interacts with the Rag GTPase complex, promoting mTORC1 inactivation under nutrient-deprived conditions by facilitating ubiquitination of RagA, thereby linking cellular energy status to metabolic adaptation. Additionally, RNF152 is implicated in autophagy and apoptosis, with studies suggesting its role in stress responses and tumor suppression. Overexpression of RNF152 inhibits cancer cell proliferation, while its downregulation correlates with poor prognosis in glioblastoma and other malignancies.
Structurally, RNF152 contains an N-terminal RING domain and a C-terminal transmembrane domain, anchoring it to membranes. Its ubiquitin ligase activity targets specific substrates for proteasomal or lysosomal degradation, influencing pathways like NF-κB signaling. Emerging evidence also connects RNF152 to neurological disorders, highlighting its broad regulatory scope. Despite progress, mechanisms underlying its substrate specificity and context-dependent roles remain under investigation, underscoring its potential as a therapeutic target in cancer and metabolic diseases.
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