首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TNF-α |
| 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 | VRSSSRTPSDKPVAHVVANPQAEGQLQWLNRRANALLANGVELRDNQLVV PSEGLYLIYSQVLFKGQGCPSTHVLLTHTISRIAVSYQTKVNLLSAIKSP CQRETPEGAEAKPWYEPIYLGGVFQLEKGDRLSAEINRPDYLDFAESGQV YFGIIAL |
| 预测分子量 | 17 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-伪重组蛋白的3篇示例文献(内容为模拟概括，实际文献需根据具体研究验证)：
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1. **文献名称**: "Engineering a Soluble TNF Receptor Fusion Protein for Anti-inflammatory Therapy"
**作者**: Smith J, et al.
**摘要**: 研究设计了一种可溶性TNF受体-IgG Fc融合蛋白(伪重组蛋白)，通过中和TNF-α活性抑制炎症反应，实验证明其在类风湿性关节炎模型中的治疗效果。
2. **文献名称**: "Mechanism of Action of a Dominant-Negative TNF Mutant in Autoimmune Disease"
**作者**: Lee C, et al.
**摘要**: 报道了一种显性负性TNF伪重组蛋白(TNF-DN)，通过竞争性结合TNF受体阻断下游信号通路，显著减轻小鼠模型中炎症性肠病的病理症状。
3. **文献名称**: "Structural and Functional Characterization of a Decoy TNF Receptor for Targeted Therapy"
**作者**: Zhang H, et al.
**摘要**: 解析了一种基于TNF受体胞外结构域的伪重组蛋白(dTNFR)的晶体结构，验证其高效抑制TNF介导的细胞凋亡和炎症因子释放的能力，为靶向治疗提供新策略。
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**备注**：以上为示例文献框架，实际引用需查询PubMed或学术数据库(如关键词：soluble TNF receptor, decoy TNF, TNF fusion protein)。经典文献可参考依那西普(Etanercept)相关研究(如Feldmann等关于TNF抑制剂的奠基性工作)。
**Background of TNF Pseudo-Recombinant Proteins**
Tumor Necrosis Factor (TNF) is a pivotal cytokine involved in systemic inflammation, immune regulation, and apoptosis. Dysregulated TNF signaling is linked to autoimmune diseases (e.g., rheumatoid arthritis, Crohn’s disease) and cancer. Therapeutic strategies often target TNF or its receptors to modulate pathological signaling. However, native TNF’s pleiotropic effects and structural complexity limit its direct therapeutic use.
TNF pseudo-recombinant proteins are engineered variants designed to mimic or antagonize TNF activity while overcoming limitations of natural TNF. These proteins are generated via recombinant DNA technology, often incorporating structural modifications such as domain truncations, point mutations, or fusion with stabilizing elements (e.g., Fc regions). For example, dominant-negative TNF mutants or soluble TNF receptor (TNFR) fusion proteins (e.g., etanercept) act as decoys to neutralize excess TNF, preventing receptor activation.
A key focus is optimizing specificity and stability. Pseudo-recombinant TNF proteins may selectively target specific TNF isoforms (e.g., soluble vs. membrane-bound TNF) or receptor subtypes (TNFR1 vs. TNFR2) to fine-tune anti-inflammatory effects while minimizing side effects like immunosuppression. Additionally, modifications enhance pharmacokinetics, such as prolonged half-life or reduced immunogenicity.
Research also explores pseudo-recombinant TNF analogs as tools to study TNF signaling mechanisms or as potential therapeutics in combination therapies. Their development bridges insights from structural biology, immunology, and protein engineering, offering tailored solutions for TNF-related pathologies. Despite challenges in clinical translation, these engineered proteins represent a versatile strategy to harness TNF biology for therapeutic benefit.
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