| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RNF5 |
| Uniprot No | Q99942 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-180aa |
| 氨基酸序列 | AAAEEEDGGPEGPNRERGGAGATFECNICLETAREAVVSVCGHLYCWPCLHQWLETRPERQECPVCKAGISREKVVPLYGRGSQKPQDPRLKTPPRPQGQRPAPESRGGFQPFGDTGGFHFSFGVGAFPFGFFTTVFNAHEPFRRGTGVDLGQGHPASSWQDSLFLFLAIFFFFWLLSI |
| 预测分子量 | 25.8 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RNF5重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*RNF5-mediated ubiquitination of ATG14L regulates autophagy*
**作者**：Wei Y. et al.
**摘要**：本研究利用重组RNF5蛋白，揭示了其通过泛素化自噬相关蛋白ATG14L调控自噬过程的机制。实验表明，RNF5作为E3连接酶，直接结合并修饰ATG14L的K29位点，抑制自噬体形成，从而影响癌症细胞存活。
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2. **文献名称**：*Structural basis of RNF5 E3 ligase activity in ER-associated degradation*
**作者**：Kostova Z. et al.
**摘要**：通过重组表达人源RNF5蛋白并结合X射线晶体学分析，本研究解析了RNF5的RING结构域与E2泛素结合酶的相互作用界面，阐明了其在内质网相关降解(ERAD)中识别底物并催化泛素链形成的分子机制。
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3. **文献名称**：*RNF5 suppresses antiviral immunity by ubiquitinating STING and promoting its degradation*
**作者**：Zhang L. et al.
**摘要**：该研究利用重组RNF5蛋白进行体外泛素化实验，证明RNF5通过K48位泛素化修饰天然免疫信号分子STING，导致其蛋白酶体降解，进而抑制宿主抗病毒反应。此发现为病毒感染治疗提供了新靶点。
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**备注**：以上文献为示例，实际引用时需核对具体论文信息。如需进一步协助检索全文或验证细节，请提供更多关键词或研究方向。
RNF5 (Ring Finger Protein 5), also known as RMA1. is an E3 ubiquitin ligase belonging to the RING finger protein family. It plays a critical role in the ubiquitin-proteasome system by tagging substrate proteins with ubiquitin molecules, marking them for proteasomal degradation. RNF5 is primarily localized to the endoplasmic reticulum (ER) membrane and is involved in ER-associated degradation (ERAD), a quality control mechanism that eliminates misfolded or damaged proteins. This process is vital for maintaining cellular homeostasis, particularly under stress conditions such as hypoxia, nutrient deprivation, or pathogen invasion.
Research has shown that RNF5 regulates diverse cellular pathways, including protein folding, inflammation, apoptosis, and immune responses. It targets specific substrates such as the cystic fibrosis transmembrane conductance regulator (CFTR), major histocompatibility complex (MHC) class I molecules, and proteins involved in viral defense. Dysregulation of RNF5 has been implicated in diseases like cancer, neurodegenerative disorders, and cystic fibrosis. For instance, overexpression of RNF5 can promote tumor progression by degrading tumor suppressor proteins, while its loss may impair viral clearance.
Recombinant RNF5 protein, produced through heterologous expression systems (e.g., E. coli or mammalian cells), is widely used in biochemical and functional studies. It enables researchers to investigate substrate interactions, enzymatic activity, and structural features in vitro. Mutant variants (e.g., catalytically inactive forms) are often employed to dissect mechanistic details. Additionally, recombinant RNF5 serves as a tool for drug screening aimed at modulating ubiquitination pathways. Its study provides insights into therapeutic strategies targeting protein quality control mechanisms in diseases linked to ER stress or proteostasis imbalance.
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