| 纯度 | >90%SDS-PAGE. |
| 种属 | mouse |
| 靶点 | SIGIRR |
| Uniprot No | Q9JLZ8-1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-238aa |
| 氨基酸序列 | MAGVCDMAPN FLSPSEDQAL GLALGREVAL NCTAWVFSRP QCPQPSVQWL KDGLALGNGS HFSLHEDFWV SANFSEIVSS VLVLNLTNAE DYGTFTCSVW NVSSHSFTLW RAGPAGHVAA VLASLLVLVV LLLVALLYVK CRLNMLLWYQ DTYGEVEMND GKLYDAYVSY SDCPEDRKFV NFILKPQLER RRGYKLFLED RDLLPRAEPS ADLLVNLSRC RRLIVVLSDA FLSRPWCS |
| 预测分子量 | 41 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SIGIRR(Single Immunoglobulin IL-1 Receptor-Related Molecule)重组蛋白的3篇代表性文献，简明概括如下：
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1. **文献名称**: *SIGIRR, a negative regulator of Toll-like receptor–interleukin 1 receptor signaling*
**作者**: Wald D, et al.
**摘要**: 该研究首次报道SIGIRR作为TLR/IL-1R信号通路的负向调控因子，通过重组蛋白实验证实其能抑制NF-κB活化，减少促炎因子产生，提示其在炎症疾病中的潜在治疗价值。
2. **文献名称**: *SIGIRR modulates the inflammatory response in human and mouse colon epithelial cells*
**作者**: Garlanda C, et al.
**摘要**: 研究利用重组SIGIRR蛋白，揭示其在肠道上皮细胞中通过阻断IL-1R/TLR信号减轻结肠炎模型中的炎症损伤，为炎症性肠病治疗提供分子机制依据。
3. **文献名称**: *Recombinant SIGIRR attenuates renal ischemia-reperfusion injury by inhibiting TLR4/NF-κB signaling*
**作者**: Leemans JC, et al.
**摘要**: 实验表明，重组SIGIRR蛋白可通过拮抗TLR4信号通路，减少肾脏缺血再灌注损伤中的炎症反应和细胞凋亡，提示其作为急性肾损伤治疗策略的可能性。
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以上研究均聚焦于SIGIRR重组蛋白的免疫调控功能，涵盖基础机制与疾病模型应用。如需更详细文献信息(期刊、年份等)，可进一步补充关键词检索。
SIGIRR (Single Immunoglobulin Interleukin-1 Receptor-Related Molecule), also known as IL-1R8 or TIR8. is a member of the interleukin-1 receptor (IL-1R) family that plays a regulatory role in innate immune responses. Structurally, it contains a single extracellular immunoglobulin (Ig) domain, a transmembrane region, and an intracellular Toll/IL-1 receptor (TIR) domain. However, unlike other IL-1R family members, SIGIRR lacks conserved residues in its TIR domain, rendering it incapable of conventional signaling. Instead, it acts as a negative regulator of Toll-like receptor (TLR) and IL-1R-mediated signaling pathways by competing for adaptor proteins or forming non-functional heterodimers with other receptors.
Discovered in the early 2000s, SIGIRR is highly expressed in epithelial tissues, including the gut, lung, and kidney, as well as in immune cells like dendritic cells. Its primary function is to dampen excessive inflammatory responses, particularly in mucosal environments exposed to microbial stimuli. Studies in SIGIRR-deficient mice have demonstrated its critical role in preventing hyperinflammatory conditions, such as colitis, sepsis, and autoimmune disorders. For example, SIGIRR knockout models exhibit exacerbated inflammation in response to TLR ligands or pathogens due to uncontrolled NF-κB and MAPK activation.
Recombinant SIGIRR protein, produced via bacterial or mammalian expression systems, has become a valuable tool for studying its immunomodulatory mechanisms. Researchers use it to explore therapeutic applications in inflammatory diseases, cancer, and sepsis. In preclinical models, administration of recombinant SIGIRR protein or gene delivery systems has shown potential in suppressing TLR/IL-1R-driven inflammation. Additionally, its interaction with key signaling components like MyD88 and IRAK is frequently analyzed using purified recombinant proteins to map inhibitory pathways. Despite progress, challenges remain in optimizing its stability and delivery for clinical use, prompting ongoing research into engineered variants or fusion proteins to enhance therapeutic efficacy.
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