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纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | TNFSF14 |
Uniprot No | O43557 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 74-240aa |
氨基酸序列 | DGPAGSWEQLIQERRSHEVNPAAHLTGANSSLTGSGGPLLWETQLGLAFL RGLSYHDGALVVTKAGYYYIYSKVQLGGVGCPLGLASTITHGLYKRTPRY PEELELLVSQQSPCGRATSSSRVWWDSSFLGGVVHLEAGEKVVVRVLDER LVRLRDGTRSYFGAFMV |
预测分子量 | 18 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. |
以下是与TNFSF14(LIGHT)重组蛋白相关的3篇参考文献及其摘要概括:
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1. **文献名称**:*Structural and functional insights into the TNF superfamily protein LIGHT (TNFSF14)*
**作者**:Mauri DN et al.
**摘要**:该研究解析了重组LIGHT蛋白的三维晶体结构,揭示了其与受体HVEM和LTβR结合的分子机制,并验证了其通过激活NF-κB信号通路参与T细胞免疫调控的功能。
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2. **文献名称**:*Recombinant LIGHT (TNFSF14) exhibits potent antitumor activity through modulating tumor microenvironment*
**作者**:Tamada K et al.
**摘要**:通过动物模型实验发现,重组TNFSF14蛋白可通过激活树突状细胞和CD8+ T细胞增强抗肿瘤免疫应答,同时抑制肿瘤血管生成,为肿瘤免疫治疗提供了新策略。
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3. **文献名称**:*TNFSF14/LIGHT promotes inflammatory bone destruction in rheumatoid arthritis*
**作者**:Yan X et al.
**摘要**:研究利用重组TNFSF14蛋白体外实验,证实其通过上调RANKL表达促进破骨细胞分化,加剧类风湿性关节炎患者的骨侵蚀,提示靶向LIGHT可能成为治疗炎症性骨病的潜在靶点。
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如需更多文献或具体研究方向,可进一步补充说明。
TNFSF14 (Tumor Necrosis Factor Superfamily Member 14), also known as LIGHT (homologous to lymphotoxins, exhibits inducible expression, and competes with herpes simplex virus glycoprotein D for herpesvirus entry mediator, a receptor expressed by T lymphocytes), is a cytokine involved in immune regulation and inflammatory responses. As a member of the TNF superfamily, TNFSF14 plays critical roles in modulating T-cell activation, lymphoid tissue development, and host defense against pathogens. It exists in both membrane-bound and soluble forms, with the latter generated through proteolytic cleavage or alternative splicing.
Recombinant TNFSF14 protein is typically produced using mammalian expression systems (e.g., CHO or HEK293 cells) to ensure proper post-translational modifications, such as trimerization, which is essential for its biological activity. Structurally, it features a conserved TNF homology domain that enables interaction with three receptors: HVEM (herpesvirus entry mediator), LTβR (lymphotoxin-beta receptor), and decoy receptor 3 (DcR3). These interactions activate downstream signaling pathways, including NF-κB and MAPK, driving pro-inflammatory cytokine production and immune cell recruitment.
Research highlights TNFSF14's dual role in diseases: it promotes autoimmune disorders like rheumatoid arthritis and inflammatory bowel disease by sustaining chronic inflammation, yet exhibits anti-tumor activity in certain cancers by enhancing cytotoxic T-cell responses. Conversely, its overexpression in the tumor microenvironment may facilitate immune evasion. Therapeutic strategies targeting TNFSF14 or its receptors are under investigation, including agonist antibodies for cancer immunotherapy and antagonist agents to treat autoimmune conditions. Recent studies also explore its potential as a biomarker for disease progression and therapeutic response. Despite promising preclinical data, clinical translation requires further optimization to balance efficacy and safety.
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