| 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.
在生物科技领域，蛋白研发与生产是前沿探索的关键支撑。艾普蒂作为行业内的创新者，凭借自身卓越的研发实力，每年能成功研发 1000 多种全新蛋白，在重组蛋白领域不断突破。 在重组蛋白生产过程中，艾普蒂积累了丰富且成熟的经验。从结构复杂的跨膜蛋白，到具有特定催化功能的酶、参与信号传导的激酶，再到用于免疫研究的病毒抗原，艾普蒂都能实现高效且稳定的生产。 这一成就离不开艾普蒂强大的技术平台。我们构建了多元化的重组蛋白表达系统，昆虫细胞、哺乳动物细胞以及原核蛋白表达系统协同运作。不同的表达系统各有优势，能够满足不同客户对重组蛋白的活性、产量、成本等多样化的需求，从而提供高品质、低成本的活性重组蛋白。 艾普蒂提供的不只是产品，更是从源头到终端的一站式解决方案。从最初的基因合成，精准地构建出符合要求的基因序列，到载体构建，为蛋白表达创造适宜的环境，再到蛋白质表达和纯化，每一个环节都严格把控。我们充分尊重客户的个性化需求，在表达 / 纯化标签的选择、表达宿主的确定等方面，为客户量身定制专属方案。 同时，艾普蒂还配备了多种纯化体系，能够应对不同特性蛋白的纯化需求。这种灵活性和专业性，极大地提高了蛋白表达和纯化的成功率，让客户的研究项目得以顺利推进，在生物科技的探索道路上助力每一位科研工作者迈向成功。
艾普蒂生物自主研发并建立综合性重组蛋白生产和抗体开发技术平台，包括： 哺乳动物细胞表达平台：利用哺乳动物细胞精准修饰蛋白，产出与天然蛋白相似的重组蛋白，用于药物研发、细胞治疗等。 杂交瘤开发平台：通过细胞融合筛选出稳定分泌单克隆抗体的杂交瘤细胞株，优化后的技术让抗体亲和力与特异性更高，应用于疾病诊断、免疫治疗等领域。 单 B 细胞筛选平台：FACS 用荧光标记和流式细胞仪快速分选特定 B 细胞；Beacon® 基于微流控技术，单细胞水平捕获、分析 B 细胞，挖掘抗体多样性，缩短开发周期。 凭借这些平台，艾普蒂生物为客户提供优质试剂和专业 CRO 技术服务，推动生物科技发展。
艾普蒂生物在重组蛋白和天然蛋白开发领域经验十分丰富，拥有超过 2 万种重组蛋白的开发案例。在四大重组蛋白表达平台的运用上，艾普蒂生物不仅经验老到，还积累了详实的成功案例。针对客户的工业化生产需求，我们能够定制并优化实验方案。通过小试探索、工艺放大以及条件优化等环节，对重组蛋白基因序列进行优化，全面探索多种条件，精准找出最契合客户需求的生产方法。 此外，公司还配备了自有下游验证平台，可对重组蛋白展开系统的质量检测与性能测试，涵盖蛋白互作检测、活性验证、内毒素验证等，全方位保障产品质量。 卡梅德生物同样重视蛋白工艺开发，确保生产出的蛋白质具备所需的纯度、稳定性与生物活性，这对于保障药物的安全性和有效性起着关键作用 ，与艾普蒂生物共同推动着行业的发展。
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