| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RNF13 |
| Uniprot No | O43567 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-381aa |
| 氨基酸序列 | MLLSIGMLMLSATQVYTILTVQLFAFLNLLPVEADILAYNFENASQTFDDLPARFGYRLPAEGLKGFLINSKPENACEPIVPPPVKDNSSGTFIVLIRRLDCNFDIKVLNAQRAGYKAAIVHNVDSDDLISMGSNDIEVLKKIDIPSVFIGESSANSLKDEFTYEKGGHLILVPEFSLPLEYYLIPFLIIVGICLILIVIFMITKFVQDRHRARRNRLRKDQLKKLPVHKFKKGDEYDVCAICLDEYEDGDKLRILPCSHAYHCKCVDPWLTKTKKTCPVCKQKVVPSQGDSDSDTDSSQEENEVTEHTPLLRPLASVSAQSFGALSESRSHQNMTESSDYEEDDNEDTDSSDAENEINEHDVVVQLQPNGERDYNIANTV |
| 预测分子量 | 42,8 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RNF13重组蛋白的3篇代表性文献及摘要概述：
1. **文献名称**：Structural and functional characterization of recombinant RNF13 E3 ubiquitin ligase
**作者**：Zhang Y, et al.
**摘要**：本研究通过大肠杆菌系统表达了重组RNF13蛋白，解析了其环指结构域的晶体结构，并证明其具有E3泛素连接酶活性。实验揭示了RNF13通过泛素化修饰调控内质网相关降解(ERAD)途径的分子机制。
2. **文献名称**：RNF13 modulates TLR4 signaling by mediating ubiquitination of TIRAP
**作者**：Wang L, et al.
**摘要**：该研究利用重组RNF13蛋白进行体外泛素化实验，发现其特异性识别并泛素化TIRAP蛋白，负向调控TLR4信号通路。这为RNF13在先天免疫中的作用提供了新证据。
3. **文献名称**：Recombinant RNF13 interacts with Bcl-2 family proteins and induces apoptosis
**作者**：Chen X, et al.
**摘要**：通过共表达纯化技术获得重组RNF13.证明其与促凋亡蛋白Bax直接结合，并通过泛素化降解抗凋亡蛋白Mcl-1.揭示了RNF13在线粒体凋亡通路中的双重调控作用。
注：以上文献信息为基于公开研究方向的模拟概括，实际文献需通过PubMed或Web of Science查询确认。
**Background of RNF13 Recombinant Protein**
RNF13 (Ring Finger Protein 13) is a member of the RING (Really Interesting New Gene) finger protein family, characterized by a conserved zinc-binding RING domain that confers E3 ubiquitin ligase activity. This enzyme plays a critical role in the ubiquitin-proteasome system (UPS), regulating protein degradation, cellular signaling, and homeostasis. RNF13 is ubiquitously expressed across tissues, with higher levels observed in the brain, heart, and immune cells, suggesting its involvement in diverse physiological processes.
Structurally, RNF13 contains an N-terminal transmembrane domain, a central RING domain, and a C-terminal region rich in proline and serine residues. It localizes primarily to endosomal and Golgi membranes, where it modulates intracellular trafficking and post-translational modifications. As an E3 ligase, RNF13 facilitates the transfer of ubiquitin molecules to substrate proteins, tagging them for proteasomal degradation or altering their interactions and activity.
Research implicates RNF13 in apoptosis, inflammation, and cancer progression. For example, it interacts with signaling pathways like NF-κB and p53. influencing cell survival and stress responses. Dysregulation of RNF13 has been linked to neurodegenerative diseases, cardiovascular disorders, and tumorigenesis, though its exact mechanisms remain under investigation.
Recombinant RNF13 protein is engineered *in vitro* using expression systems (e.g., *E. coli* or mammalian cells) to produce purified, functional protein for mechanistic studies. This tool enables researchers to analyze its enzymatic activity, substrate specificity, and structural features. Applications include studying UPS-related pathologies, screening for small-molecule inhibitors, or exploring its role in disease models. Tags (e.g., His or GST tags) are often added to facilitate purification and detection.
Overall, RNF13 recombinant protein serves as a vital resource for deciphering the molecular pathways governed by this E3 ligase and its potential as a therapeutic target.
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