| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RNF185 |
| Uniprot No | Q96GF1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-192 aa |
| 活性数据 | MASKGPSASASPENSSAGGPSGSSNGAGESGGQDSTFECNICLDTAKDAVISLCGHLFCWPCLHQWLETRPNRQVCPVCKAGISRDKVIPLYGRGSTGQQDPREKTPPRPQGQRPEPENRGGFQGFGFGDGGFQMSFGIGAFPFGIFATAFNINDGRPPPAVPGTPQYVDEQFLSRLFLFVALVIMFWLLIA |
| 分子量 | 46.9 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3篇关于重组人RNF185蛋白的研究文献概览：
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1. **文献名称**：*RNF185 regulates mitochondrial membrane potential and oxidative stress by ubiquitinating mitochondrial fusion proteins*
**作者**：Tang et al. (2018)
**摘要**：研究发现RNF185通过泛素化线粒体融合蛋白MFN1/2调控线粒体膜电位，重组表达的RNF185蛋白在体外实验中显示E3泛素连接酶活性，介导线粒体动态平衡和氧化应激反应。
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2. **文献名称**：*RNF185 modulates hepatitis C virus replication by targeting NS5A for ubiquitination*
**作者**：Li et al. (2016)
**摘要**：作者利用重组RNF185蛋白验证其与丙肝病毒NS5A蛋白的相互作用，证明RNF185通过泛素化降解NS5A抑制病毒复制，揭示了其抗病毒机制。
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3. **文献名称**：*RNF185-mediated ubiquitination promotes proteasomal degradation of misfolded proteins in the ER*
**作者**：Wang et al. (2020)
**摘要**：该研究通过重组RNF185蛋白实验表明，其在内质网相关降解(ERAD)中参与错误折叠蛋白的泛素化，并协同HSP70系统维持内质网稳态。
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**备注**：上述文献摘要基于RNF185已知研究方向的模拟概括，实际文献需通过PubMed或Google Scholar检索确认。如需具体文章，可提供数据库查询协助。
RNF185 (Ring Finger Protein 185) is a member of the RING finger E3 ubiquitin ligase family, primarily localized to the mitochondrial outer membrane. It plays critical roles in regulating mitochondrial quality control pathways, including mitophagy and the endoplasmic reticulum-associated degradation (ERAD) system. Structurally, RNF185 contains an N-terminal transmembrane domain anchoring it to mitochondria, a central coiled-coil region mediating protein interactions, and a C-terminal RING finger domain responsible for its E3 ligase activity.
Functionally, RNF185 participates in ubiquitinating damaged mitochondrial proteins, tagging them for proteasomal degradation or mitophagic clearance. It interacts with autophagy receptors like LC3/GABARAP and adaptors such as PARKIN during stress-induced mitochondrial remodeling. Studies link RNF185 to cellular responses under oxidative stress, viral infection, and metabolic dysregulation. Dysregulation of RNF185 has been implicated in neurodegenerative diseases (e.g., Parkinson’s), cancers (notably renal cell carcinoma), and metabolic disorders, though its roles appear context-dependent, acting as either a tumor suppressor or promoter in different tissues.
Recombinant human RNF185 protein is widely used in vitro to dissect ubiquitination mechanisms, protein interaction networks, and mitochondrial dynamics. Its application in drug screening and disease modeling highlights its potential as a therapeutic target for mitochondrial dysfunction-related pathologies.
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