纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | RNF4 |
Uniprot No | P78317 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-190aa |
氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMSTRKRR GGAINSRQAQ KRTREATSTP EISLEAEPIE LVETAGDEIV DLTCESLEPV VVDLTHNDSV VIVDERRRPR RNARRLPQDH ADSCVVSSDD EELSRDRDVY VTTHTPRNAR DEGATGLRPS GTVSCPICMD GYSEIVQNGR LIVSTECGHV FCSQCLRDSL KNANTCPTCR KKINHKRYHP IYI |
预测分子量 | 24 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RNF4重组蛋白的3篇参考文献及其摘要内容:
1. **文献名称**:*RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation*
**作者**:Tatham, M.H. et al.
**摘要**:该研究发现RNF4重组蛋白通过识别SUMO化修饰的底物(如PML蛋白),介导其多聚泛素化降解,揭示了RNF4在砷剂诱导白血病治疗中的关键作用。
2. **文献名称**:*The SUMO-targeted ubiquitin ligase RNF4 regulates the localization and function of the DNA repair protein 53BP1*
**作者**:Sun, Y. et al.
**摘要**:研究利用重组RNF4蛋白证明其通过SUMO-泛素双重调控机制,影响53BP1在DNA损伤位点的聚集,从而调节同源重组修复过程。
3. **文献名称**:*Recombinant RNF4 expression and purification: Insights into its structural and functional modularity*
**作者**:Hakli, M. et al.
**摘要**:该文献报道了RNF4重组蛋白在大肠杆菌中的高效表达和纯化方法,并分析其SIM结构域(SUMO相互作用模体)与RING结构域在底物识别和泛素化中的协同机制。
RNF4 (Ring Finger Protein 4) is a ubiquitin E3 ligase that plays a critical role in regulating protein homeostasis, DNA damage response, and cellular stress pathways. It belongs to the RING finger family of proteins, characterized by a conserved C3HC4-type zinc-binding RING domain essential for mediating ubiquitin transfer. RNF4 specifically recognizes and ubiquitinates proteins modified by SUMO (Small Ubiquitin-like Modifier), a process termed SUMO-targeted ubiquitination (STUbL). This activity links SUMOylation to proteasomal degradation, enabling the selective removal of SUMO-conjugated proteins involved in DNA repair, transcriptional regulation, and genomic stability.
Recombinant RNF4 protein is engineered for in vitro studies to dissect its molecular mechanisms. It is typically produced in bacterial (e.g., *E. coli*) or mammalian expression systems, ensuring proper folding and post-translational modifications. The recombinant form retains key functional domains: the N-terminal SIMs (SUMO-interacting motifs) for binding poly-SUMO chains and the C-terminal RING domain for E3 ligase activity. Researchers utilize it to study substrate recognition, ubiquitination kinetics, and interactions with components of the ubiquitin-proteasome system.
RNF4's role in diseases, particularly cancer and neurodegenerative disorders, has driven interest in its recombinant form. Dysregulation of RNF4 is linked to impaired DNA repair (e.g., in BRCA-mutant cancers) and accumulation of toxic protein aggregates. Recombinant RNF4 facilitates drug screening to identify modulators of its activity, offering therapeutic potential. Its study also advances understanding of post-translational modification crosstalk, a hallmark of cellular signaling networks.
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