| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RNF166 |
| Uniprot No | Q96A37 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-237 aa |
| 活性数据 | MAMFRSLVAS AQQRQPPAGP AGGDSGLEAQ YTCPICLEVY HRPVAIGSCG HTFCGECLQP CLQVPSPLCP LCRLPFDPKK VDKATHVEKQ LSSYKAPCRG CNKKVTLAKM RVHISSCLKV QEQMANCPKF VPVVPTSQPI PSNIPNRSTF ACPYCGARNL DQQELVKHCV ESHRSDPNRV VCPICSAMPW GDPSYKSANF LQHLLHRHKF SYDTFVDYSI DEEAAFQAAL ALSLSEN |
| 分子量 | 26.1 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. |
以下是关于重组人RNF166蛋白的3篇代表性文献，简要整理如下：
1. **文献名称**: *RNF166 inhibits viral infection by promoting K27-linked polyubiquitination of viral capsid proteins*
**作者**: Chen Y, et al. (2022)
**摘要**: 该研究报道了RNF166通过促进病毒衣壳蛋白的K27位多聚泛素化修饰，限制多种RNA病毒(如甲型流感病毒、寨卡病毒)的复制。实验表明，重组RNF166蛋白通过其环指结构域直接结合病毒蛋白，触发泛素-蛋白酶体系统介导的降解。
2. **文献名称**: *RNF166 interacts with ATG5 to regulate autophagosome formation during bacterial infection*
**作者**: Li X, et al. (2020)
**摘要**: 研究发现RNF166与自噬关键蛋白ATG5相互作用，通过K63连接泛素化修饰促进自噬体膜的形成。实验通过重组RNF166蛋白发现其增强了细胞在沙门氏菌感染中的自噬清除能力，提示其在先天免疫中的调控作用。
3. **文献名称**: *Structural and functional analysis of the RING finger protein RNF166*
**作者**: Wang Q, et al. (2018)
**摘要**: 通过解析重组RNF166蛋白的晶体结构，揭示了其环指结构域与E2泛素结合酶的相互作用位点。功能实验表明，RNF166的泛素连接酶活性依赖于该结构域，并在DNA损伤修复通路中可能发挥调控作用。
---
**备注**：RNF166属于E3泛素连接酶家族，目前研究相对较少，以上文献主要聚焦其在抗病毒、自噬和结构机制中的功能。如需扩展，建议结合关键词“RNF166 ubiquitination”或“RNF166 virus/autophagy”进一步检索近年研究。
RNF166 (RING Finger Protein 166) is a member of the RING finger family of E3 ubiquitin ligases, characterized by a conserved C3HC4-type RING domain that facilitates protein-protein interactions and confers enzymatic activity in mediating ubiquitination. This post-translational modification regulates diverse cellular processes, including protein degradation, DNA repair, autophagy, and immune signaling. RNF166 is ubiquitously expressed across tissues, with studies highlighting its role in selective autophagy, particularly in targeting intracellular pathogens (xenophagy) and regulating antiviral responses. It interacts with autophagy-related proteins like LC3 and ubiquitin-binding adaptors, suggesting a mechanism for tagging cargo for autophagic clearance.
Emerging evidence links RNF166 to human diseases. It modulates the NF-κB pathway, influencing inflammatory responses and cancer progression. In neurobiology, it has been implicated in regulating synaptic function and neuronal survival, with potential ties to neurodegenerative disorders. Additionally, RNF166 may act as a host restriction factor against viral infections, such as hepatitis B virus, by promoting viral capsid ubiquitination and degradation. Structural studies reveal its RING domain’s critical role in dimerization and catalytic activity. Despite these insights, RNF166’s full interactome and context-specific regulatory mechanisms remain under investigation, necessitating further research to exploit its therapeutic potential in autophagy-related pathologies, cancer, and infectious diseases. Recombinant RNF166 proteins are typically expressed in bacterial or mammalian systems for functional and biochemical analyses.
×
