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 | TNF, |
| Uniprot No | P01375 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 77-233aa |
| 氨基酸序列 | VRSSSRTPSDKPVAHVVANPQAEGQLQWLNRRANALLANGVELRDNQLVVPSEGLYLIYSQVLFKGQGCPSTHVLLTHTISRIAVSYQTKVNLLSAIKSPCQRETPEGAEAKPWYEPIYLGGVFQLEKGDRLSAEINRPDYLDFAESGQVYFGIIAL |
| 预测分子量 | 19.4 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TNF(肿瘤坏死因子)和重组蛋白的3篇经典参考文献摘要：
1. **文献名称**：*Tumor necrosis factor: a cytokine involved in toxic effects of endotoxin*
**作者**：Beutler, B., & Cerami, A.
**摘要**：该研究阐明了TNF-α在细菌内毒素(如LPS)引发的炎症反应中的核心作用，揭示了重组TNF蛋白在实验模型中模拟内毒素毒性的能力，为脓毒症机制研究提供了关键依据。
2. **文献名称**：*Cloning and expression in Escherichia coli of the cDNA for human tumor necrosis factor*
**作者**：Pennica, D., et al.
**摘要**：首次报道了人TNF-α基因的克隆及在大肠杆菌中的高效重组表达，证明了重组TNF蛋白具有与天然蛋白相同的生物活性(如诱导肿瘤细胞凋亡)，为后续治疗性开发奠定基础。
3. **文献名称**：*Structure of tumour necrosis factor*
**作者**：Eck, M.J., & Sprang, S.R.
**摘要**：通过X射线晶体学解析了重组TNF-α的三维结构，揭示其三聚体构象及与受体结合的分子机制，为设计靶向TNF的药物(如抑制剂依那西普)提供了结构生物学依据。
4. **文献名称**：*TNF in the regulation of immune cells in health and disease*
**作者**：Sedger, L.M., & McDermott, M.F.
**摘要**：综述了重组TNF蛋白在免疫调节中的双重作用(如促进炎症/抗肿瘤 vs. 诱发自身免疫病)，并讨论了基于重组TNF或抗TNF疗法(如英夫利昔单抗)的临床应用及挑战。
以上文献覆盖了TNF的功能机制、重组表达技术、结构解析及临床应用，适用于基础研究与生物技术开发参考。
**Tumor Necrosis Factor (TNF)** is a pro-inflammatory cytokine primarily produced by immune cells, such as macrophages and T lymphocytes. Discovered in the 1970s for its ability to induce tumor cell death, TNF plays a central role in regulating immune responses, inflammation, and apoptosis. It exists in two forms: soluble (sTNF) and membrane-bound (mTNF), both signaling through TNF receptors (TNFR1 and TNFR2) to activate pathways like NF-κB and MAPK. While essential for host defense, dysregulated TNF production is linked to autoimmune diseases (e.g., rheumatoid arthritis, Crohn’s disease) and chronic inflammatory conditions, making it a key therapeutic target.
**Recombinant proteins** are artificially engineered proteins produced via genetic engineering in host systems (e.g., bacteria, yeast, mammalian cells). This technology allows large-scale production of proteins with precise modifications, enabling therapeutic and research applications. For TNF-related studies, recombinant TNF (rTNF) is used to investigate its biological roles or screen inhibitors. Conversely, recombinant TNF inhibitors (e.g., etanercept, a TNFR-Fc fusion protein) are biologics designed to neutralize excessive TNF activity, revolutionizing treatment for autoimmune diseases. Beyond therapeutics, recombinant proteins are vital tools in structural biology, drug discovery, and diagnostics, highlighting their versatility in bridging basic research and clinical innovation. The development of TNF-targeted recombinant biologics underscores the intersection of cytokine biology and protein engineering in modern medicine.
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