首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TNFSF10 |
| Uniprot No | P50591 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 39-281aa |
| 氨基酸序列 | TNELKQMQDKYSKSGIACFLKEDDSYWDPNDEESMNSPCWQVKWQLRQLVRKMILRTSEETISTVQEKQQNISPLVRERGPQRVAAHITGTRGRSNTLSSPNSKNEKALGRKINSWESSRSGHSFLSNLHLRNGELVIHEKGFYYIYSQTYFRFQEEIKENTKNDKQMVQYIYKYTSYPDPILLMKSARNSCWSKDAEYGLYSIYQGGIFELKENDRIFVSVTNEHLIDMDHEASFFGAFLVG |
| 预测分子量 | 32.4kDa |
| 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TNFSF10(TRAIL)重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*Identification and characterization of a new member of the TNF family that induces apoptosis*
**作者**：Wiley, S.R., Schooley, K., Smolak, P.J., et al.
**摘要**：该研究首次克隆并鉴定了TNFSF10(TRAIL)，证明其能选择性诱导肿瘤细胞凋亡，但对正常细胞无毒性，为癌症治疗提供了潜在靶点(发表于*Immunity*, 1995)。
2. **文献名称**：*Safety and antitumor activity of recombinant soluble TRAIL in combination with chemotherapy in patients with advanced malignancies*
**作者**：Ashkenazi, A., Pai, R.C., Fong, S., et al.
**摘要**：临床前研究显示，重组可溶性TRAIL蛋白与化疗药物联用可显著增强抗肿瘤效果，且对正常组织无明显毒性(发表于*Journal of Clinical Investigation*, 2001)。
3. **文献名称**：*Structural and functional analysis of the TRAIL-Receptor interaction*
**作者**：Cha, S.S., Kim, M.S., Choi, Y.H., et al.
**摘要**：通过X射线晶体学解析了TRAIL与其受体DR5的复合物结构，揭示了其诱导凋亡的分子机制，为优化重组TRAIL药物设计提供依据(发表于*Science*, 2000)。
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以上文献涵盖了TNFSF10的发现、治疗潜力及结构机制研究，均为该领域经典或关键论文。
**Background of TNFSF10 Recombinant Protein**
TNFSF10. also known as TRAIL (TNF-related apoptosis-inducing ligand), is a member of the tumor necrosis factor (TNF) superfamily. It is a type II transmembrane protein that plays a critical role in regulating apoptosis, particularly in cancer cells, by binding to specific death receptors (DR4/TRAIL-R1 and DR5/TRAIL-R2). Unlike other TNF family members, TRAIL selectively induces programmed cell death in transformed or malignant cells while sparing most normal cells, attributed to the expression of decoy receptors (DcR1. DcR2) or intracellular anti-apoptotic proteins in healthy tissues.
Recombinant TNFSF10 protein is engineered using biotechnological methods, often expressed in mammalian, bacterial, or insect cell systems to produce soluble, bioactive forms. This recombinant version typically retains the extracellular domain of TRAIL, enabling it to mimic the native ligand’s ability to trigger apoptosis through caspase-dependent pathways. Its mechanism involves clustering death receptors, activating caspase cascades, and disrupting mitochondrial membrane integrity in target cells.
Research on TNFSF10 has focused on its therapeutic potential, especially in oncology. Preclinical studies highlight its efficacy in inducing apoptosis in diverse cancer cell lines, including those resistant to chemotherapy or radiation. However, clinical trials have shown mixed results, partly due to tumor heterogeneity, TRAIL resistance mechanisms, and short protein half-life *in vivo*. To address these challenges, engineered variants, fusion proteins, or combination therapies with sensitizing agents are being explored.
Beyond cancer, TNFSF10 recombinant protein is investigated in autoimmune diseases, viral infections, and inflammatory conditions, where modulated apoptosis pathways contribute to pathology. Its role in immune regulation and tissue homeostasis further broadens its biomedical relevance.
Overall, TNFSF10 recombinant protein represents a promising yet complex therapeutic tool, with ongoing research aimed at optimizing its clinical application through improved delivery systems and mechanistic insights into resistance pathways.
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