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 | TNFA |
| 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. |
以下是与TNFA(Tumor Necrosis Factor Alpha)重组蛋白相关的3-4篇文献摘要概览：
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1. **文献名称**：*Human tumor necrosis factor: Production, purification, and characterization*
**作者**：Aggarwal, B.B. et al.
**摘要**：该研究报道了通过基因工程技术在大肠杆菌中高效表达重组人TNF-α的方法，并详细描述了其纯化流程与生物活性验证。研究发现重组TNF-α在体外实验中可诱导肿瘤细胞凋亡，为后续抗肿瘤研究奠定基础(*Journal of Biological Chemistry*, 1985)。
2. **文献名称**：*Crystal structure of TNF-α mutant reveals key structural determinants for receptor binding*
**作者**：Banner, D.W. et al.
**摘要**：通过X射线晶体学解析TNF-α突变体的三维结构，揭示了其与细胞表面受体结合的分子机制，为设计靶向TNF-α的抑制剂(如抗体药物)提供了结构依据(*Nature*, 1993)。
3. **文献名称**：*Recombinant TNF-α in cancer therapy: Preclinical and clinical perspectives*
**作者**：Balkwill, F.
**摘要**：综述了重组TNF-α在肿瘤治疗中的潜力，包括其促炎与促凋亡作用，同时讨论了高剂量毒性问题及局部给药(如肿瘤内注射)的优化策略(*Nature Reviews Cancer*, 2009)。
4. **文献名称**：*PEGylated recombinant human TNF-α: Pharmacokinetics and antitumor efficacy*
**作者**：van Horssen, P.J. et al.
**摘要**：研究通过聚乙二醇(PEG)修饰重组TNF-α以延长其半衰期，并在动物模型中验证了修饰后蛋白的增强抗肿瘤效果与降低的全身毒性(*Biomaterials*, 2010)。
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**说明**：上述文献涵盖了TNFA重组蛋白的生产、结构解析、治疗应用及药物改良等方向，均为领域内代表性研究。实际引用时建议通过PubMed或学术数据库核对完整信息。
**Background of Recombinant TNFA Protein**
Tumor Necrosis Factor-alpha (TNF-α), a pivotal cytokine in immune regulation, was first identified in 1975 for its ability to induce tumor cell death. It is primarily produced by macrophages, T-cells, and other immune cells, playing a central role in inflammation, apoptosis, and host defense. Dysregulated TNF-α signaling is linked to autoimmune diseases (e.g., rheumatoid arthritis, Crohn’s disease) and chronic inflammatory conditions, making it a critical therapeutic target.
Recombinant TNF-α (rTNF-α) proteins are engineered using genetic cloning techniques, often expressed in *E. coli* or mammalian cell systems to ensure proper folding and bioactivity. The mature TNF-α protein exists as a homotrimer, binding to TNF receptors (TNFR1/TNFR2) to activate downstream pathways like NF-κB and MAPK, which regulate immune responses and cell survival.
The development of rTNF-α revolutionized biomedical research, enabling mechanistic studies of TNF-mediated pathways and drug discovery. Notably, anti-TNF therapies (e.g., monoclonal antibodies like infliximab, soluble receptors like etanercept) emerged as breakthrough treatments for autoimmune diseases by neutralizing excessive TNF-α activity. Conversely, recombinant TNF-α itself has been explored in cancer therapy, leveraging its cytotoxic effects, though systemic toxicity limits clinical use.
Today, rTNF-α remains a vital tool for studying inflammation, immune modulation, and cell death, while anti-TNF biologics represent one of the most successful applications of cytokine-targeted therapeutics. Ongoing research focuses on optimizing TNF-α-based strategies to balance efficacy and safety in diverse pathologies.
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