| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PELI1 |
| Uniprot No | Q96FA3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-418aa |
| 氨基酸序列 | MFSPDQENHPSKAPVKYGELIVLGYNGSLPNGDRGRRKSRFALFKRPKANGVKPSTVHIACTPQAAKAISNKDQHSISYTLSRAQTVVVEYTHDSNTDMFQIGRSTESPIDFVVTDTVPGSQSNSDTQSVQSTISRFACRIICERNPPFTARIYAAGFDSSKNIFLGEKAAKWKTSDGQMDGLTTNGVLVMHPRNGFTEDSKPGIWREISVCGNVFSLRETRSAQQRGKMVEIETNQLQDGSLIDLCGATLLWRTAEGLSHTPTVKHLEALRQEINAARPQCPVGFNTLAFPSMKRKDVVDEKQPWVYLNCGHVHGYHNWGNKEERDGKDRECPMCRSVGPYVPLWLGCEAGFYVDAGPPTHAFSPCGHVCSEKTTAYWSQIPLPHGTHTFHAACPFCAHQLAGEQGYIRLIFQGPLD |
| 预测分子量 | 73.0 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3-4条与**PELI1重组蛋白**相关的参考文献及其简要摘要内容：
1. **《PELI1-mediated ubiquitination modifies TLR signaling in innate immunity》**
*作者：Smith J, et al.*
摘要：研究利用重组PELI1蛋白，揭示了其作为E3泛素连接酶在TLR信号通路中的调控作用，通过促进关键蛋白的泛素化增强炎症因子(如TNF-α和IL-6)的产生。
2. **《PELI1重组蛋白调控T细胞活化的分子机制》**
*作者：Wang L, et al.*
摘要：通过体外表达纯化的PELI1重组蛋白，证实其与TCR信号通路中的关键激酶(如TAK1)相互作用，负向调控T细胞过度活化，影响自身免疫疾病进程。
3. **《Structural insights into PELI1’s role in necroptosis via RIPK1 ubiquitination》**
*作者：Chen X, et al.*
摘要：解析重组PELI1蛋白的晶体结构，发现其通过介导RIPK1的K63泛素化修饰，促进坏死性凋亡(necroptosis)信号传导，为靶向PELI1的炎症治疗提供依据。
4. **《PELI1重组蛋白在病毒逃逸宿主免疫中的功能研究》**
*作者：Kim S, et al.*
摘要：利用重组PELI1蛋白进行体外实验，证明其通过降解MAVS蛋白抑制I型干扰素通路，揭示病毒利用宿主PELI1逃避免疫监视的新机制。
(注：以上文献为示例性概括，实际引用需根据具体研究内容匹配真实文献。)
**Background of PELI1 Recombinant Protein**
PELI1 (pellino E3 ubiquitin protein ligase 1) is a member of the Pellino family of E3 ubiquitin ligases, which play critical roles in regulating immune and inflammatory signaling pathways. Structurally, PELI1 contains an N-terminal RING-like domain responsible for its E3 ligase activity and C-terminal NPL4 zinc finger domains that mediate substrate interactions. It functions as a key modulator of innate and adaptive immunity, primarily through ubiquitination-dependent regulation of signaling molecules.
PELI1 is best known for its involvement in Toll-like receptor (TLR) and interleukin-1 receptor (IL-1R) pathways, where it ubiquitinates proteins such as TRAF3 and IRAK1. influencing downstream NF-κB and MAPK activation. This activity links PELI1 to pro-inflammatory cytokine production, T-cell activation, and immune homeostasis. Dysregulation of PELI1 has been implicated in autoimmune diseases (e.g., rheumatoid arthritis, multiple sclerosis), neurodegenerative disorders, and cancers. In oncology, PELI1 exhibits dual roles—acting as an oncogene by promoting tumor cell survival or as a tumor suppressor depending on cellular context.
Recombinant PELI1 protein is produced using expression systems (e.g., *E. coli* or mammalian cells) to study its biochemical properties, substrate interactions, and enzymatic activity *in vitro*. Tagged versions (e.g., His, GST) facilitate purification and detection. Researchers employ this tool to dissect PELI1’s role in ubiquitination cascades, screen for inhibitors, or explore its therapeutic potential in inflammation-related diseases and cancer. Its study provides insights into developing targeted therapies for immune dysregulation and malignancies.
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