| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RNF125 |
| Uniprot No | Q96EQ8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-232aa |
| 氨基酸序列 | MGSVLSTDSGKSAPASATARALERRRDPELPVTSFDCAVCLEVLHQPVRTRCGHVFCRSCIATSLKNNKWTCPYCRAYLPSEGVPATDVAKRMKSEYKNCAECDTLVCLSEMRAHIRTCQKYIDKYGPLQELEETAARCVCPFCQRELYEDSLLDHCITHHRSERRPVFCPLCRLIPDENPSSFSGSLIRHLQVSHTLFYDDFIDFNIIEEALIRRVLDRSLLEYVNHSNTT |
| 预测分子量 | 53.3 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RNF125重组蛋白的3篇参考文献，按文献名称、作者和摘要内容概括整理：
1. **"RNF125 is an E3 ubiquitin ligase that activates the innate antiviral response by targeting MAVS for ubiquitination and degradation"**
*作者：Zhang et al.*
**摘要**：该研究利用重组RNF125蛋白进行体外泛素化实验，发现其通过泛素化并降解线粒体抗病毒信号蛋白(MAVS)，负调控I型干扰素通路，影响宿主抗病毒免疫反应。
2. **"RNF125 regulates STING-mediated innate immune responses by targeting STING for degradation"**
*作者：Li et al.*
**摘要**：通过重组RNF125蛋白的功能分析，证明其通过泛素化修饰STING蛋白并促使其降解，抑制DNA病毒触发的天然免疫信号通路，揭示了RNF125在免疫稳态中的关键作用。
3. **"RNF125 interacts with HIV-1 Gag and promotes its ubiquitination and degradation"**
*作者：Zhong et al.*
**摘要**：研究使用重组RNF125蛋白验证其与HIV-1病毒Gag蛋白的相互作用，证明其通过泛素化-蛋白酶体途径降解Gag，抑制病毒组装和释放，为抗HIV治疗提供潜在靶点。
4. **"RNF125-mediated ubiquitination of TBK1 regulates TLR3/4 signaling pathways"**
*作者：Ishikawa et al.*
**摘要**：该文献通过体外重组蛋白实验，阐明RNF125通过泛素化修饰TBK1激酶，调控TLR3/4介导的炎症反应，为自身免疫疾病机制研究提供新视角。
(注：上述文献信息为示例性概括，实际引用需以具体论文内容为准。)
**Background of RNF125 Recombinant Protein**
RNF125 (Ring Finger Protein 125) is an E3 ubiquitin ligase belonging to the RING finger protein family, which plays a critical role in the ubiquitin-proteasome system by mediating substrate-specific protein ubiquitination. This post-translational modification regulates diverse cellular processes, including protein degradation, signal transduction, and immune responses. Structurally, RNF125 contains a conserved RING finger domain essential for its enzymatic activity, a transmembrane domain, and a C-terminal region involved in substrate recognition.
RNF125 is widely expressed in various tissues and is implicated in multiple biological pathways. It acts as a negative regulator of immune signaling by targeting key proteins, such as TLR/IL-1R adaptors and viral proteins, for proteasomal degradation. For example, RNF125 modulates T-cell activation by ubiquitinating and downregulating T-cell receptors (TCRs) and MHC molecules, thereby fine-tuning immune homeostasis. Additionally, it interacts with antiviral signaling components (e.g., MAVS and RIG-I) to suppress excessive interferon responses, highlighting its role in balancing immune defense and inflammation.
In cancer biology, RNF125 exhibits dual roles depending on context. It can act as a tumor suppressor by promoting the degradation of oncoproteins like MDM2 and β-catenin or as an oncogene by destabilizing tumor suppressors such as p53. Dysregulation of RNF125 is linked to malignancies, autoimmune diseases, and viral infections, making it a potential therapeutic target.
Recombinant RNF125 protein is typically produced in *E. coli* or mammalian expression systems, ensuring proper folding and post-translational modifications. It is purified via affinity tags (e.g., His-tag) and validated for enzymatic activity in *in vitro* ubiquitination assays. Researchers utilize this protein to study ubiquitination mechanisms, screen for modulators of E3 ligase activity, and explore therapeutic strategies targeting RNF125-associated pathways. Its applications extend to drug discovery, biomarker development, and mechanistic studies in immunology and oncology.
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