| 纯度 | >97%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TIFA |
| Uniprot No | Q9GZX6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 34-179aa |
| 氨基酸序列 | M+APISSHCRL DKSNFQQPYI TNRTFMLAKE ASLADNNTDV RLIGEKLFHG VSMSERCYLM KQVLNFTLEE VLFPQSDRFQ PYMQEVVPFL ARLSNRLSTC HIEGDDLHIQ RNVQKLKDTV KKLGESGEIK AIGELDLLFM SLRNACI |
| 预测分子量 | 16.9kDa |
| 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. |
以下是关于TIFA重组蛋白的参考文献示例(注：以下内容为示例性概括，具体文献请通过学术数据库核实)：
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1. **文献名称**：*Structural insights into TIFA oligomerization and its role in innate immune signaling*
**作者**：Huang Y. et al.
**摘要**：本研究解析了重组人源TIFA蛋白的晶体结构，揭示了其通过FHA结构域介导的寡聚化机制，并证明该过程在激活下游NF-κB信号通路中起关键作用，为炎症反应的分子机制提供了新见解。
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2. **文献名称**：*TIFA-dependent sensing of bacterial pathogens through metabolic perturbation*
**作者**：Li X. et al.
**摘要**：文章通过重组TIFA蛋白体外实验，发现其可识别细菌代谢中间产物ADP-庚糖，诱导TIFA寡聚化并触发炎症小体活化，阐明了TIFA在宿主防御中的代谢传感功能。
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3. **文献名称**：*Recombinant TIFA expression in E. coli and functional analysis in hepatocellular carcinoma*
**作者**：Wang Q. et al.
**摘要**：报道了在大肠杆菌中高效表达可溶性重组TIFA蛋白的方法，并发现其在肝癌细胞中通过调控ERK信号通路抑制肿瘤生长，提示其潜在的治疗应用价值。
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4. **文献名称**：*TIFA as a mediator of DNA damage-induced NF-κB activation*
**作者**：Goto T. et al.
**摘要**：研究利用重组TIFA突变体证明，其FHA结构域与TRAF6的结合是DNA损伤后触发NF-κB活化和细胞凋亡的必要条件，揭示了TIFA在基因组稳定性维持中的双重作用。
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**注意**：以上文献信息为基于研究领域典型内容的示例，实际引用时请通过PubMed、Google Scholar等平台检索并核实具体文献DOI及发表年份。
**Background of TIFA Recombinant Protein**
TIFA (TRAF-interacting protein with forkhead-associated domain) is a cytosolic adaptor protein involved in innate immune signaling, particularly in the activation of the NF-κB pathway. It contains an N-terminal forkhead-associated (FHA) domain, which mediates phospho-specific protein interactions, and a C-terminal TRAF6-binding motif. TIFA plays a critical role in sensing metabolic or pathogenic stress, such as heme-induced oxidative stress or bacterial infection, by oligomerizing upon phosphorylation or ubiquitination. This oligomerization facilitates the recruitment and activation of TRAF6. a ubiquitin ligase essential for downstream NF-κB and MAPK signaling, leading to pro-inflammatory cytokine production.
Recombinant TIFA protein is engineered using expression systems like *E. coli* or mammalian cells, often fused with tags (e.g., His, GST) for purification and detection. Its production enables detailed study of TIFA’s structure-function relationships, post-translational modifications (e.g., Thr9 phosphorylation), and interactions with partners like TRAF6 or caspase-8. Researchers use it to dissect mechanisms underlying immune dysregulation, cancer progression (e.g., hepatocellular carcinoma), or microbial pathogenesis.
TIFA’s role in bridging cellular stress to inflammatory responses makes it a potential therapeutic target. Recombinant variants, including mutants (e.g., phospho-defective T9A), help identify signaling nodes for drug development. Its applications span *in vitro* binding assays, structural studies (e.g., crystallography), and cell-based models to explore pathways linked to inflammation, apoptosis, and infection. Overall, TIFA recombinant protein serves as a vital tool for unraveling immune signaling complexity and advancing translational research.
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