纯度 | >90%SDS-PAGE. |
种属 | E.coli |
靶点 | RNF1 |
Uniprot No | P10282 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-131aa |
氨基酸序列 | MLFFKSIASLAALVSLAVASPIESRQSATTCGSTNYSASQVRAAANAACQYYQNDDTAGSSTYPHTYNNYEGFDFPVDGPYQEFPIKSGGVYTGGSPGADRVVINTNCEYAGAITHTGASGNNFVGCSGTN |
预测分子量 | 13,6 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RNF1重组蛋白的3篇参考文献示例(注:部分内容为模拟文献,实际引用时需核实具体信息):
1. **文献名称**:*RNF1 mediates ubiquitination and degradation of BRCA1 in DNA damage response*
**作者**:Smith J, et al.
**摘要**:本研究利用重组RNF1蛋白揭示了其在DNA损伤修复中的作用,证明RNF1通过泛素化修饰BRCA1并促进其蛋白酶体降解,从而调控同源重组修复效率。
2. **文献名称**:*Structural and functional characterization of recombinant RNF1 E3 ligase*
**作者**:Li X, et al.
**摘要**:该研究通过表达纯化重组人源RNF1蛋白,解析其晶体结构,并验证其体外泛素化活性,揭示了其Ring结构域对底物识别和催化机制的关键作用。
3. **文献名称**:*RNF1 regulates autophagy by ubiquitinating LC3 in mammalian cells*
**作者**:Chen Y, et al.
**摘要**:利用重组RNF1蛋白进行体外实验,发现其通过K63-linked泛素化修饰LC3蛋白,调控自噬小体形成,影响细胞在营养胁迫下的存活。
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**提示**:实际研究中建议通过PubMed或Web of Science等平台,以“RNF1 recombinant protein”或“RNF1 ubiquitin ligase”为关键词检索最新文献,优先选择近五年内的高影响力期刊论文。
**Background of RNF1 Recombinant Protein**
RNF1 (Ring Finger Protein 1) is a member of the E3 ubiquitin ligase family, characterized by a conserved RING (Really Interesting New Gene) domain that facilitates substrate recognition and ubiquitin transfer. It plays a critical role in the ubiquitin-proteasome system (UPS), regulating protein degradation, cellular homeostasis, and signaling pathways. RNF1-mediated ubiquitination typically targets proteins for proteasomal degradation, influencing processes such as DNA repair, cell cycle progression, apoptosis, and immune responses. Dysregulation of RNF1 has been implicated in various pathologies, including cancer, neurodegenerative diseases, and inflammatory disorders, highlighting its therapeutic relevance.
Recombinant RNF1 protein is engineered using molecular cloning techniques, often expressed in *E. coli* or mammalian cell systems to ensure proper folding and post-translational modifications. Purification methods (e.g., affinity chromatography with His-tags) yield high-purity protein for functional studies. Researchers utilize recombinant RNF1 to investigate its enzymatic activity, substrate specificity, and interactions with co-factors (e.g., E2 ubiquitin-conjugating enzymes) in *in vitro* assays. It also serves as a tool to study UPS dysregulation in disease models or to screen for inhibitors/activators in drug discovery.
Recent studies emphasize RNF1's role in modulating immune signaling (e.g., NF-κB pathways) and tumor suppression, making it a potential biomarker or target for therapies. Its recombinant form accelerates mechanistic insights and translational applications, bridging molecular biology with clinical research.
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