| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PELI3 |
| Uniprot No | Q8N2H9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-469aa |
| 氨基酸序列 | MVLEGNPEVGSPRTSDLQHRGNKGSCVLSSPGEDAQPGEEPIKYGELIVLGCCEEGGEETEAQRGEVTGPRAHSCYNGCLASGDKGRRRSRLALSRRSHANGVKPDVMHHISTPLVSKALSNRGQHSISYTLSRSHSVIVEYTHDSDTDMFQIGRSTENMIDFVVTDTSPGGGAAEGPSAQSTISRYACRILCDRRPPYTARIYAAGFDASSNIFLGERAAKWRTPDGLMDGLTTNGVLVMHPAGGFSEDSAPGVWREISVCGNVYTLRDSRSAQQRGKLVENESNVLQDGSLIDLCGATLLWRTPAGLLRAPTLKQLEAQRQEANAARPQCPVGLSTLAFPSPARGRTAPDKQQPWVYVRCGHVHGYHGWGCRRERGPQERECPLCRLVGPYVPLWLGQEAGLCLDPGPPSHAFAPCGHVCSEKTARYWAQTPLPHGTHAFHAACPFCGAWLTGEHGCVRLIFQGPLD |
| 预测分子量 | 54.8 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. |
以下是假设的关于PELI3重组蛋白的模拟参考文献(实际文献需通过学术数据库验证)：
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1. **文献名称**: *PELI3 regulates TLR4-mediated inflammatory response via ubiquitination of IRAK1*
**作者**: Chen X, Li Y, et al. (2021)
**摘要**: 研究阐明了PELI3重组蛋白通过泛素化修饰IRAK1分子调控TLR4信号通路，影响巨噬细胞炎症因子释放的分子机制，为败血症治疗提供潜在靶点。
2. **文献名称**: *Structural characterization of recombinant PELI3 and its role in cancer cell apoptosis*
**作者**: Wang H, Zhang R, et al. (2020)
**摘要**: 通过体外表达纯化PELI3重组蛋白，解析其晶体结构，并证明其在非小细胞肺癌中通过调控MAPK通路诱导肿瘤细胞凋亡的功能。
3. **文献名称**: *PELI3 deficiency exacerbates autoimmune encephalomyelitis by enhancing Th17 differentiation*
**作者**: Kim S, Jung J, et al. (2022)
**摘要**: 利用PELI3重组蛋白进行体外功能回补实验，发现其通过抑制RORγt泛素化降解负向调节Th17细胞分化，在多发性硬化症小鼠模型中具有保护作用。
4. **文献名称**: *Recombinant PELI3 as a potential biomarker in rheumatoid arthritis*
**作者**: Müller P, Schmidt E, et al. (2019)
**摘要**: 临床样本分析显示，PELI3重组蛋白在类风湿关节炎患者滑膜液中高表达，且与疾病活动度正相关，提示其作为炎症标志物的潜力。
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**注意**：以上摘要为模拟内容，真实研究需参考PubMed、Web of Science等平台的具体文献。
**Background of PELI3 Recombinant Protein**
PELI3 (Pellino E3 Ubiquitin Protein Ligase Family Member 3) is a member of the Pellino family of E3 ubiquitin ligases, which play critical roles in regulating innate immune signaling and inflammatory responses. The Pellino family, including PELI1. PELI2. and PELI3. is evolutionarily conserved and primarily involved in modulating Toll-like receptor (TLR) and interleukin-1 receptor (IL-1R) signaling pathways. PELI3. specifically, acts as a key mediator in post-translational modifications, catalyzing the attachment of ubiquitin molecules to target proteins, thereby influencing their stability, localization, or activity.
Structurally, PELI3 contains a conserved N-terminal forkhead-associated (FHA) domain for phospho-dependent protein interactions and a C-terminal RING-like domain responsible for its E3 ligase activity. This enables PELI3 to participate in ubiquitination cascades, often regulating downstream effectors such as NF-κB and MAPK pathways, which are central to immune and stress responses. Studies suggest PELI3 may have dual roles—promoting or inhibiting inflammation depending on cellular context—highlighting its functional complexity.
Recombinant PELI3 protein, produced via heterologous expression systems (e.g., *E. coli* or mammalian cells), retains these biochemical properties and is widely used to investigate molecular mechanisms in vitro. Researchers employ it to study interactions with substrates like IRAK1 (Interleukin-1 Receptor-Associated Kinase 1) or TRAF6 (TNF Receptor-Associated Factor 6), decipher ubiquitination patterns, and explore its regulatory impact on immune signaling. Dysregulation of PELI3 has been implicated in autoimmune diseases, cancers, and infections, making it a potential therapeutic target.
Despite progress, PELI3's full physiological relevance remains under investigation. Its recombinant form continues to serve as a vital tool for unraveling its role in immunity, inflammation, and disease pathogenesis.
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