| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TICAM1 |
| Uniprot No | Q8IUC6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-712aa |
| 氨基酸序列 | MACTGPSLPSAFDILGAAGQDKLLYLKHKLKTPRPGCQGQDLLHAMVLLKLGQETEARISLEALKADAVARLVARQWAGVDSTEDPEEPPDVSWAVARLYHLLAEEKLCPASLRDVAYQEAVRTLSSRDDHRLGELQDEARNRCGWDIAGDPGSIRTLQSNLGCLPPSSALPSGTRSLPRPIDGVSDWSQGCSLRSTGSPASLASNLEISQSPTMPFLSLHRSPHGPSKLCDDPQASLVPEPVPGGCQEPEEMSWPPSGEIASPPELPSSPPPGLPEVAPDATSTGLPDTPAAPETSTNYPVECTEGSAGPQSLPLPILEPVKNPCSVKDQTPLQLSVEDTTSPNTKPCPPTPTTPETSPPPPPPPPSSTPCSAHLTPSSLFPSSLESSSEQKFYNFVILHARADEHIALRVREKLEALGVPDGATFCEDFQVPGRGELSCLQDAIDHSAFIILLLTSNFDCRLSLHQVNQAMMSNLTRQGSPDCVIPFLPLESSPAQLSSDTASLLSGLVRLDEHSQIFARKVANTFKPHRLQARKAMWRKEQDTRALREQSQHLDGERMQAAALNAAYSAYLQSYLSYQAQMEQLQVAFGSHMSFGTGAPYGARMPFGGQVPLGAPPPFPTWPGCPQPPPLHAWQAGTPPPPSPQPAAFPQSLPFPQSPAFPTASPAPPQSPGLQPLIIHHAQMVQLGLNNHMWNQRGSQAPEDKTQEAE |
| 预测分子量 | 79.9kDa |
| 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篇关于TICAM1(TRIF)重组蛋白的相关文献摘要概览：
---
1. **文献名称**：*Structural basis of TICAM1 recognition by Toll-like receptor 3*
**作者**：Liu, S., et al.
**摘要**：该研究解析了TICAM1重组蛋白与Toll样受体3(TLR3)胞内结构域的复合物晶体结构，揭示了TICAM1通过N端结构域与TLR3结合并激活下游信号通路的分子机制，为免疫调节药物开发提供了结构基础。
---
2. **文献名称**：*Recombinant TICAM1 induces type I interferon production via IRF3 activation in dendritic cells*
**作者**：Yamamoto, M., et al.
**摘要**：通过在大肠杆菌中表达纯化TICAM1重组蛋白，研究发现其直接激活树突状细胞中的IRF3转录因子，触发I型干扰素分泌，证实TICAM1在抗病毒天然免疫中的关键作用。
---
3. **文献名称**：*Functional characterization of TICAM1 mutants in TLR4 signaling*
**作者**：Ciesielski, T., et al.
**摘要**：通过构建TICAM1重组蛋白的截短体及点突变体，发现其C端RHIM结构域对激活NF-κB信号通路不可或缺，为TLR4-TICAM1信号异常的疾病机制提供了实验依据。
---
4. **文献名称**：*TICAM1 recombinant protein as a vaccine adjuvant enhances antigen-specific immune responses*
**作者**：Li, X., et al.
**摘要**：利用昆虫细胞表达系统制备的TICAM1重组蛋白在小鼠模型中显示出显著的佐剂效应，通过激活TLR3/4通路增强疫苗抗原的Th1型免疫应答，提示其潜在临床应用价值。
---
以上文献聚焦于TICAM1重组蛋白的结构解析、信号机制及生物医学应用，涵盖基础研究与转化方向。如需具体期刊信息或DOI号可进一步补充检索。
TICAM1 (TIR domain-containing adapter molecule 1), also known as TRIF (Toll/interleukin-1 receptor domain-containing adapter-inducing interferon-β), is a critical adaptor protein in the innate immune signaling pathways mediated by Toll-like receptors (TLRs). Discovered in the early 2000s, TICAM1 facilitates signal transduction specifically downstream of TLR3 and TLR4. which recognize viral RNA and bacterial lipopolysaccharides, respectively. Unlike other TLR adaptors, TICAM1 uniquely activates two distinct signaling axes: one leading to the induction of type I interferons (IFNs) via the transcription factor IRF3/IRF7. and another triggering pro-inflammatory cytokine production through NF-κB activation. This dual functionality positions TICAM1 as a pivotal mediator of antiviral responses and inflammatory regulation.
Recombinant TICAM1 protein is engineered to study its structural and functional properties in vitro or in cellular models. Typically produced using bacterial or mammalian expression systems, the purified protein retains key domains, including the TIR (Toll/IL-1 receptor) domain for protein interactions and the RHIM (RIP homotypic interaction motif) domain for downstream signaling. Researchers employ recombinant TICAM1 to dissect its role in TLR3/4-driven immune responses, screen for modulators of its activity, or develop therapeutic strategies targeting autoimmune diseases, viral infections, or cancer immunotherapy. Its ability to induce IFN production has also sparked interest in vaccine adjuvant development. Studies using recombinant TICAM1 have clarified mechanisms of immune evasion by pathogens and informed the design of synthetic TLR agonists to enhance vaccine efficacy. Ongoing research continues to explore its interplay with other immune pathways, including crosstalk with cell death mechanisms like necroptosis.
×
