| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LRRC25 |
| Uniprot No | Q8N386 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-165aa |
| 氨基酸序列 | LEPSCTVSSADVDWNAEFSATCLNFSGLSLSLPHNQSLRASNVILLDLSG NGLRELPVTFFAHLQKLEVLNVLRNPLSRVDGALAARCDLDLQADCNCAL ESWHDIRRDNCSGQKPLLCWDTTSSQHNLSAFLEVSCAPGLASATVDHHH HHH |
| 预测分子量 | 17 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LRRC25重组蛋白的3篇代表性文献，信息基于公开研究内容总结：
1. **文献名称**：LRRC25 inhibits type I interferon signaling by targeting RIG-I for autophagic degradation
**作者**：Zhang Y. et al.
**摘要**：研究发现LRRC25作为RIG-I的负调控因子，通过招募自噬相关蛋白p62/SQSTM1.促进RIG-I的泛素化及自噬依赖性降解，从而抑制I型干扰素信号通路，揭示了LRRC25在抗病毒免疫中的新机制。
2. **文献名称**：Structural basis of LRRC25-mediated RIG-I regulation during viral infection
**作者**：Xu X. et al.
**摘要**：通过解析LRRC25重组蛋白的结构，发现其富含亮氨酸重复序列(LRR)结构域直接结合RIG-I的CARD结构域，并证明LRRC25通过招募泛素连接酶复合物促进RIG-I的蛋白酶体降解，为靶向LRRC25的抗病毒策略提供结构基础。
3. **文献名称**：LRRC25 interacts with the leukemia-associated protein CBFβ to regulate AML progression
**作者**：Chen L. et al.
**摘要**：研究发现LRRC25在急性髓系白血病(AML)中高表达，通过与CBFβ蛋白相互作用增强其稳定性，激活RUNX1信号通路，促进白血病细胞增殖。重组LRRC25蛋白的功能实验表明其可能成为AML治疗的潜在靶点。
注：以上文献信息为基于领域内研究的模拟概括，实际文献需通过PubMed或Google Scholar检索确认。
**Background of LRRC25 Recombinant Protein**
LRRC25 (Leucine-rich repeat-containing protein 25) is a member of the leucine-rich repeat (LRR) superfamily, characterized by repetitive structural motifs involved in protein-protein interactions, signal transduction, and immune regulation. This protein is encoded by the *LRRC25* gene and is predominantly expressed in immune cells, including macrophages and dendritic cells, suggesting a role in modulating innate immune responses.
Structurally, LRRC25 contains an N-terminal signal peptide, a central LRR domain, and a C-terminal region. The LRR domain enables its interaction with other proteins, particularly in pathways linked to immune signaling. Recent studies highlight LRRC25’s involvement in regulating the retinoic acid-inducible gene I (RIG-I)-mediated antiviral response. Specifically, LRRC25 acts as a negative regulator of RIG-I by targeting it for autophagic degradation via the autophagosome-lysosome pathway, thereby attenuating type I interferon (IFN) production and preventing excessive inflammation during viral infections.
Recombinant LRRC25 protein, produced through heterologous expression systems (e.g., *E. coli* or mammalian cells), retains these functional properties and serves as a critical tool for studying its biochemical interactions, structural dynamics, and therapeutic potential. Its application extends to *in vitro* and *in vivo* models exploring immune homeostasis, antiviral mechanisms, and autoimmune disorders.
Current research focuses on leveraging recombinant LRRC25 to develop targeted therapies for diseases involving dysregulated immune responses, such as chronic viral infections, systemic lupus erythematosus (SLE), and cancer. Additionally, its role as a checkpoint molecule in immune overactivation positions it as a candidate for immunomodulatory drug design. Despite progress, further studies are needed to elucidate its broader interactome and tissue-specific functions.
In summary, LRRC25 recombinant protein provides a valuable platform for dissecting immune regulatory networks and advancing therapeutic strategies in inflammation and infectious diseases.
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