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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TNFSF12 |
| Uniprot No | O43508 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 93-249aa |
| 氨基酸序列 | RSAPKGRKTRARRAIAAHYEVHPRPGQDGAQAGVDGTVSGWEEARINSSS PLRYNRQIGEFIVTRAGLYYLYCQVHFDEGKAVYLKLDLLVDGVLALRCL EEFSATAASSLGPQLRLCQVSGLLALRPGSSLRIRTLPWAHLKAAPFLTY FGLFQVH |
| 预测分子量 | 17 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TNFSF12(TWEAK)重组蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**: *TWEAK, a new secreted ligand in the tumor necrosis factor family that weakly induces apoptosis*
**作者**: Chicheportiche, Y. 等
**摘要**: 该研究首次克隆并表达了重组TNFSF12(TWEAK)蛋白，证明其属于TNF超家族，可通过结合受体FN14诱导部分肿瘤细胞系凋亡，但在正常细胞中活性较弱，提示其选择性作用机制。
2. **文献名称**: *Structural basis for the interaction of the cytokine TWEAK with its receptor FN14*
**作者**: Brown, S.A. 等
**摘要**: 通过X射线晶体学解析重组TNFSF12蛋白与其受体FN14的复合物结构，揭示了二者结合的关键位点，为开发靶向TNFSF12/FN14通路的药物(如癌症或炎症疾病治疗)提供了结构基础。
3. **文献名称**: *Recombinant TWEAK enhances inflammation-driven tumor progression via NF-κB activation in a preclinical model of pancreatic cancer*
**作者**: Li, H. 等
**摘要**: 研究利用重组TNFSF12蛋白在胰腺癌小鼠模型中验证其促炎作用，发现其通过激活NF-κB通路促进肿瘤微环境中炎症因子释放，加速肿瘤进展，提示抑制TNFSF12可能具有治疗潜力。
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以上文献涵盖TNFSF12重组蛋白的早期功能发现、结构机制及疾病模型应用，可作为相关研究的参考基础。如需具体文献年份或期刊信息，可进一步通过PubMed/Google Scholar检索标题或作者。
TNFSF12. also known as TWEAK (TNF-related weak inducer of apoptosis), is a member of the tumor necrosis factor (TNF) superfamily. This cytokine plays a multifaceted role in regulating cellular processes such as apoptosis, proliferation, inflammation, and tissue repair. The native TNFSF12 protein is a type II transmembrane protein that can be proteolytically processed into a soluble form, enabling interaction with its primary receptor, Fn14 (TNFRSF12A). This ligand-receptor interaction activates downstream signaling pathways, including NF-κB and MAPK, influencing immune responses and tissue homeostasis.
Recombinant TNFSF12 is engineered using expression systems like mammalian cells or *E. coli* to produce purified, bioactive proteins for research and therapeutic development. The recombinant form typically retains the functional epitopes required for receptor binding, allowing scientists to study its biological effects in vitro and in vivo. Its applications span cancer research, autoimmune diseases, and regenerative medicine, as TNFSF12 exhibits context-dependent roles—promoting apoptosis in certain tumor cells while driving pro-inflammatory responses or tissue remodeling in others.
Studies highlight its dual nature: excessive TNFSF12/Fn14 signaling is implicated in chronic inflammation, fibrosis, and cancer progression, yet it also shows potential in enhancing wound healing and neuroprotection. Researchers utilize recombinant TNFSF12 to dissect these mechanisms, develop biomarkers, or explore targeted therapies. Inhibitors blocking TNFSF12-Fn14 interactions are under investigation for conditions like rheumatoid arthritis and solid tumors, while recombinant TNFSF12 itself is explored for regenerative applications. Its versatility underscores its importance in both pathophysiology and translational medicine.
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