| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TNFRSF12A |
| Uniprot No | Q9NP84 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 28-80aa |
| 氨基酸序列 | EQAPGTAPCS RGSSWSADLD KCMDCASCRA RPHSDFCLGC AAAPPAPFRL LWP |
| 预测分子量 | 5.6 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TNFRSF12A(FN14)重组蛋白的3篇参考文献示例：
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1. **"TNFRSF12A/FN14 signaling in cancer: Functional insights and therapeutic targeting"**
- **作者**: Winkles JA, et al.
- **摘要**: 研究了TNFRSF12A重组蛋白在肿瘤微环境中的促癌作用，通过激活NF-κB通路促进肿瘤细胞增殖和转移，提出靶向FN14的潜在治疗策略。
2. **"Crystal structure of the TWEAK-FN14 complex reveals insights into receptor activation"**
- **作者**: Brown SA, et al.
- **摘要**: 解析了重组TNFRSF12A蛋白与配体TWEAK的复合物晶体结构，揭示了配体结合诱导受体三聚化的分子机制，为靶向药物设计提供结构基础。
3. **"Recombinant FN14 extracellular domain attenuates renal fibrosis in mice by blocking TWEAK signaling"**
- **作者**: Michaelson JS, et al.
- **摘要**: 利用重组TNFRSF12A胞外域蛋白抑制TWEAK-FN14信号通路，在小鼠模型中显著减轻肾脏纤维化，验证了其作为治疗慢性纤维化疾病的潜力。
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以上文献涵盖基础机制、结构研究和临床应用方向，均涉及TNFRSF12A重组蛋白的功能或实验应用。如需具体年份或期刊信息可进一步补充。
TNFRSF12A, also known as FN14 or TWEAK receptor, is a member of the tumor necrosis factor receptor superfamily (TNFRSF). This cell surface receptor is encoded by the TNFRSF12A gene and plays a critical role in regulating cellular responses such as proliferation, survival, inflammation, and tissue remodeling. It binds to its ligand TWEAK (TNF-like weak inducer of apoptosis), triggering downstream signaling pathways, including NF-κB and MAPK, which influence diverse physiological and pathological processes.
Structurally, TNFRSF12A is a type I transmembrane protein containing a cysteine-rich extracellular domain critical for ligand interaction and a cytoplasmic tail lacking intrinsic enzymatic activity. Instead, it recruits adaptor proteins to mediate intracellular signaling. While expressed at low levels in healthy tissues, its expression is upregulated in conditions involving tissue injury, chronic inflammation, fibrosis, and cancer. This dynamic regulation links TNFRSF12A to diseases such as hepatocellular carcinoma, glioblastoma, rheumatoid arthritis, and fibrotic disorders.
Recombinant TNFRSF12A protein is engineered in vitro using expression systems (e.g., mammalian, bacterial) to produce purified, functional forms of the receptor for research. It serves as a tool to study receptor-ligand interactions, signaling mechanisms, and therapeutic targeting. For example, recombinant proteins enable screening for inhibitors blocking TWEAK/FN14 signaling, a pathway implicated in tumor progression and resistance to therapy. Additionally, they facilitate structural studies to map binding interfaces or develop diagnostic assays.
Therapeutic interest in TNFRSF12A stems from its dual role: promoting tissue repair in acute injury but driving pathological remodeling in chronic diseases. Recombinant variants, including soluble decoy receptors, are being explored to neutralize TWEAK activity in inflammatory and oncologic contexts. However, challenges remain in balancing therapeutic efficacy with potential off-target effects due to the receptor's broad biological roles.
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