首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TRAIL |
| Uniprot No | P50591 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 95-281aa |
| 氨基酸序列 | TSEETISTVQEKQQNISPLVRERGPQRVAAHITGTRGRSNTLSSPNSKNE KALGRKINSWESSRSGHSFLSNLHLRNGELVIHEKGFYYIYSQTYFRFQE EIKENTKNDKQMVQYIYKYTSYPDPILLMKSARNSCWSKDAEYGLYSIYQ GGIFELKENDRIFVSVTNEHLIDMDHEASFFGAFLVG |
| 预测分子量 | 22 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. |
1. **文献名称**：*Identification and characterization of a new member of the TNF family that induces apoptosis*
**作者**：Wiley, S.R., et al.
**摘要**：该研究首次克隆并鉴定了TRAIL(TNF相关凋亡诱导配体)，发现其能选择性诱导转化细胞或肿瘤细胞凋亡，但对正常细胞无明显毒性，提示其作为抗癌治疗的潜力。
2. **文献名称**：*TRAIL-R1 and TRAIL-R2: Receptors for TRAIL with potential for cancer therapy*
**作者**：Walczak, H., et al.
**摘要**：研究阐明了TRAIL通过结合死亡受体TRAIL-R1(DR4)和TRAIL-R2(DR5)激活凋亡信号通路的机制，并验证了重组TRAIL蛋白在体外和动物模型中诱导肿瘤细胞凋亡的效果。
3. **文献名称**：*Safety and antitumor activity of recombinant soluble Apo2 ligand*
**作者**：Ashkenazi, A., et al.
**摘要**：报道了重组可溶性Apo2L/TRAIL蛋白的临床前研究，证明其通过激活凋亡通路抑制肿瘤生长，且对正常细胞无显著毒性，支持其进入临床试验。
4. **文献名称**：*Targeting death receptors in cancer with Apo2L/TRAIL*
**作者**：Johnstone, R.W., et al.
**摘要**：综述总结了重组TRAIL蛋白的分子机制及临床研究进展，讨论了其在实体瘤和血液肿瘤中的疗效，同时分析了耐药性机制及联合用药策略。
Tumor Necrosis Factor-Related Apoptosis-Inducing Ligand (TRAIL), also known as Apo2L, is a cytokine identified in the mid-1990s as a member of the tumor necrosis factor (TNF) superfamily. It is a type II transmembrane protein that can be cleaved into a soluble form, both of which bind to specific death receptors (DR4/TRAIL-R1 and DR5/TRAIL-R2) on the cell surface. TRAIL selectively induces apoptosis in transformed or cancerous cells while sparing most normal cells, a unique feature that sparked interest in its potential as a cancer therapeutic. This selectivity arises from the differential expression of decoy receptors (DcR1. DcR2) and intracellular apoptotic regulators in normal versus malignant cells.
Recombinant TRAIL refers to engineered versions of this protein produced via genetic engineering in systems like *E. coli*, yeast, or mammalian cells. Early preclinical studies demonstrated its ability to trigger caspase-mediated apoptosis in diverse cancer cell lines and xenograft models. However, clinical trials with recombinant TRAIL or TRAIL receptor agonists showed mixed results, partly due to resistance mechanisms in tumors, such as downregulation of death receptors, overexpression of anti-apoptotic proteins (e.g., FLIP, Bcl-2), or insufficient drug delivery.
Despite these challenges, TRAIL remains a compelling candidate for targeted cancer therapy. Current research focuses on combination strategies with chemotherapeutics, radiation, or other biologics to sensitize resistant tumors. Additionally, novel delivery systems, including nanoparticle-conjugated TRAIL or gene therapy approaches, aim to enhance stability and tumor-specific targeting. Beyond oncology, TRAIL’s role in immune regulation and inflammatory diseases is under exploration. Its dual capacity to kill malignant cells and modulate the tumor microenvironment continues to drive translational studies aiming to harness its full therapeutic potential.
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