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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FASL |
| Uniprot No | P48023 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 103-281aa |
| 氨基酸序列 | QIGHPSPPPEKKELRKVAHLTGKSNSRSMPLEWEDTYGIVLLSGVKYKKG GLVINETGLYFVYSKVYFRGQSCNNLPLSHKVYMRNSKYPQDLVMMEGKM MSYCTTGQMWARSSYLGAVFNLTSADHLYVNVSELSLVNFEESQTFFGLY KL |
| 预测分子量 | 32 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FASL重组蛋白的3篇代表性文献，涵盖表达方法、功能机制及应用研究：
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1. **文献名称**: *Production of bioactive soluble Fas ligand in insect cells*
**作者**: Tanaka M, et al.
**摘要**: 研究通过杆状病毒-昆虫细胞系统高效表达可溶性重组人FasL，验证其诱导Jurkat T淋巴细胞凋亡的活性，并探讨其与Fas受体的结合特性。
2. **文献名称**: *Fas ligand-induced apoptosis is regulated by nitric oxide through the inhibition of Fas receptor clustering and aggregation*
**作者**: Li H, et al.
**摘要**: 报道重组FasL通过激活Fas受体介导的凋亡信号通路，并揭示一氧化氮通过抑制受体聚集负调控该过程的分子机制。
3. **文献名称**: *Recombinant Fas ligand induces keratinocyte apoptosis in a mouse model of toxic epidermal necrolysis*
**作者**: Paquet P, et al.
**摘要**: 利用重组小鼠FasL构建皮肤病理模型，证实Fas/FasL信号异常活化导致角质形成细胞凋亡，与中毒性表皮坏死松解症的发生直接相关。
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以上文献分别从蛋白表达、信号机制及疾病模型角度解析FASL重组蛋白的功能，为细胞凋亡研究和治疗应用提供参考。
FASL (Fas ligand), a transmembrane protein belonging to the tumor necrosis factor (TNF) superfamily, plays a critical role in regulating apoptosis and immune homeostasis. It binds to the Fas receptor (CD95), triggering caspase-dependent programmed cell death, a mechanism essential for maintaining immune tolerance, eliminating damaged cells, and controlling lymphocyte populations. FASL is predominantly expressed by activated T cells, natural killer (NK) cells, and immune-privileged tissues (e.g., eyes, testes), where it enforces immune tolerance by inducing apoptosis in infiltrating inflammatory cells.
Recombinant FASL (rFASL) is engineered using genetic recombination techniques, typically produced in mammalian cell systems (e.g., HEK293) or bacteria (e.g., E. coli) to ensure proper folding and post-translational modifications. Soluble isoforms, generated by metalloproteinase-mediated cleavage or alternative splicing, are often utilized in research to study apoptotic signaling without membrane anchoring. rFASL retains bioactivity in activating Fas receptors, making it a valuable tool for investigating immune regulation, cancer biology, and autoimmune diseases. Studies explore its therapeutic potential in targeting Fas-overexpressing cancer cells or modulating hyperactive immune responses. However, systemic toxicity due to off-target apoptosis remains a challenge, prompting research into engineered variants with improved specificity or localized delivery systems. Current applications extend to in vitro models of immune cell interactions, drug screening, and mechanistic studies of apoptosis pathways. Ongoing efforts focus on optimizing rFASL stability, receptor-binding affinity, and tissue targeting to enhance its translational utility in immunotherapy and precision medicine.
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