| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TRAF1 |
| Uniprot No | Q13077 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-416aa |
| 氨基酸序列 | MASSSGSSPRPAPDENEFPFGCPPTVCQDPKEPRALCCAGCLSENPRNGE DQICPKCRGEDLQSISPGSRLRTQEKAHPEVAEAGIGCPFAGVGCSFKGS PQSVQEHEVTSQTSHLNLLLGFMKQWKARLGCGLESGPMALEQNLSDLQL QAAVEVAGDLEVDCYRAPCSESQEELALQHFMKEKLLAELEGKLRVFENI VAVLNKEVEASHLALATSIHQSQLDRERILSLEQRVVELQQTLAQKDQAL GKLEQSLRLMEEASFDGTFLWKITNVTRRCHESACGRTVSLFSPAFYTAK YGYKLCLRLYLNGDGTGKRTHLSLFIVIMRGEYDALLPWPFRNKVTFMLL DQNNREHAIDAFRPDLSSASFQRPQSETNVASGCPLFFPLSKLQSPKHAY VKDDTMFLKCIVETST |
| 预测分子量 | 74 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TRAF1重组蛋白的3篇参考文献示例(注：以下为虚构内容，实际文献需通过数据库验证)：
1. **文献名称**：*Structural and functional analysis of TRAF1 in NF-κB signaling*
**作者**：Häcker, G., et al.
**摘要**：本研究利用重组TRAF1蛋白解析其与TNF受体复合物的结合机制，揭示了TRAF1通过特定结构域调控NF-κB信号通路的分子基础。
2. **文献名称**：*TRAF1 synergizes with TRAF2 in CD40-mediated apoptosis resistance*
**作者**：Arch, R.H., et al.
**摘要**：通过重组TRAF1和TRAF2蛋白的共表达实验，证明两者协同抑制CD40信号诱导的细胞凋亡，为癌症治疗提供潜在靶点。
3. **文献名称**：*Recombinant TRAF1 protein modulates TLR3-dependent immune responses*
**作者**：Hostager, B.S., et al.
**摘要**：利用大肠杆菌表达系统纯化重组TRAF1蛋白，发现其通过TLR3通路调控干扰素产生，揭示了其在抗病毒免疫中的新功能。
建议通过PubMed或Google Scholar搜索真实文献，关键词如“TRAF1 recombinant protein”或“TRAF1 signaling”。
TRAF1 (TNF receptor-associated factor 1) is a member of the TRAF protein family, which plays critical roles in mediating signal transduction pathways involved in immune response, inflammation, and apoptosis. Discovered in 1994. TRAF1 is distinct from other TRAF members (TRAF2-6) as it lacks the N-terminal RING finger domain but retains the C-terminal TRAF domain required for protein-protein interactions. It primarily functions as an adaptor molecule, linking cell surface receptors like TNF receptors (TNFRs), CD40. and 4-1BB to downstream signaling cascades, particularly the NF-κB and MAPK pathways. TRAF1 is highly expressed in lymphoid tissues and regulates cell survival, proliferation, and stress responses, with dual roles in promoting or inhibiting apoptosis depending on cellular context.
Recombinant TRAF1 proteins are engineered using expression systems like *E. coli* or mammalian cells to study its structure-function relationships, interaction networks, and regulatory mechanisms. These proteins typically include tags (e.g., His-tag, GST) for purification and detection. Research using recombinant TRAF1 has revealed its involvement in immune disorders, viral infections (e.g., EBV, HCV), and cancers. For example, TRAF1 overexpression is linked to lymphoma progression and resistance to chemotherapy, while its deficiency exacerbates autoimmune conditions like rheumatoid arthritis. Structural studies highlight its TRAF domain’s role in trimerization and binding to receptor cytoplasmic regions or other signaling proteins.
Current applications of recombinant TRAF1 include deciphering its role in TNF-mediated inflammation, optimizing therapeutic strategies targeting TRAF-dependent pathways, and exploring its potential as a biomarker. Its interplay with TRAF2 and cellular inhibitors of apoptosis (cIAPs) remains a focus in developing treatments for cancer and chronic inflammatory diseases. Despite progress, questions persist about its context-dependent signaling outcomes and tissue-specific regulatory mechanisms, driving ongoing research using recombinant protein tools.
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