| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TNFRSF1A |
| Uniprot No | P19438 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 30-211aa |
| 氨基酸序列 | LVPHLGDREK RDSVCPQGKY IHPQNNSICC TKCHKGTYLY NDCPGPGQDT DCRECESGSF TASENHLRHC LSCSKCRKEM GQVEISSCTV DRDTVCGCRK NQYRHYWSEN LFQCFNCSLC LNGTVHLSCQ EKQNTVCTCH AGFFLRENEC VSCSNCKKSL ECTKLCLPQI ENVKGTEDSG TT |
| 预测分子量 | 21 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3篇与TNFRSF1A重组蛋白相关的代表性文献摘要(内容为模拟概括，非真实文献)：
1. **标题**：Crystal structure of the TNFRSF1A extracellular domain in complex with TNFα
**作者**：Smith A, et al.
**摘要**：通过X射线晶体学解析了TNFRSF1A胞外结构域与TNFα结合的分子机制，揭示了受体-配体相互作用的关键氨基酸残基，为开发靶向抑制剂奠定结构基础。
2. **标题**：Recombinant soluble TNFRSF1A attenuates inflammatory responses in murine sepsis models
**作者**：Chen L, et al.
**摘要**：研究重组可溶性TNFRSF1A蛋白在脓毒症小鼠模型中的抗炎作用，证明其通过竞争性结合TNFα显著降低促炎因子水平并提高生存率。
3. **标题**：Functional characterization of a TNFR1 (TNFRSF1A) mutation associated with TRAPS syndrome
**作者**：Garcia-Carbonell R, et al.
**摘要**：利用重组TNFRSF1A蛋白研究肿瘤坏死因子受体相关周期性综合征(TRAPS)相关突变对NF-κB信号通路的异常激活机制，揭示突变导致受体自发性聚集。
4. **标题**：Production of bioactive TNFRSF1A in a mammalian expression system
**作者**：Wang Y, et al.
**摘要**：报道一种基于HEK293细胞的高效重组TNFRSF1A蛋白表达纯化策略，验证其体外结合TNFα的活性及稳定性，适用于高通量药物筛选。
注：以上为示例性内容，实际文献需通过PubMed/Google Scholar检索关键词"TNFRSF1A recombinant protein"或"TNFR1 recombinant"获取。
**Background of TNFRSF1A Recombinant Protein**
TNFRSF1A (tumor necrosis factor receptor superfamily member 1A), also known as TNFR1 or CD120a, is a cell surface receptor that binds tumor necrosis factor-alpha (TNF-α) and lymphotoxin-alpha, playing a central role in regulating inflammation, apoptosis, and immune responses. It is a type I transmembrane protein comprising an extracellular domain with cysteine-rich motifs for ligand binding, a transmembrane region, and a cytoplasmic death domain critical for signaling. TNFRSF1A activation triggers pathways like NF-κB and MAPK, influencing cell survival, cytokine production, and tissue homeostasis. Dysregulation of TNFRSF1A signaling is linked to autoimmune diseases, cancer, and neurodegenerative disorders.
Recombinant TNFRSF1A protein is engineered using expression systems (e.g., mammalian, insect, or bacterial cells) to produce soluble or membrane-bound forms for research and therapeutic applications. The recombinant version often includes the extracellular domain to study ligand-receptor interactions or block pathological TNF-α activity. Its production involves cloning the gene sequence into expression vectors, followed by purification via affinity chromatography (e.g., His-tag or Fc-fusion methods). Quality control assays (SDS-PAGE, Western blot, ELISA) ensure purity, stability, and bioactivity.
This protein is widely used to investigate TNF-α signaling mechanisms, screen anti-inflammatory drugs, and develop biologics like decoy receptors or neutralizing antibodies. In therapeutics, recombinant TNFRSF1A derivatives (e.g., etanercept analogs) have been explored to neutralize excess TNF-α in conditions such as rheumatoid arthritis. Additionally, it serves as a tool to study genetic mutations (e.g., in TRAPS syndrome) that impair receptor function. By enabling precise manipulation of TNF pathways, TNFRSF1A recombinant protein remains vital for advancing immunology research and targeted therapies.
×
