| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TR1 |
| Uniprot No | Q8IYR6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 40-330aa |
| 氨基酸序列 | SNQPPGGGGGSGGDCPGGKGKSINCSELNVRESDVRVCDESSCKYGGVCKEDGDGLKCACQFQCHTNYIPVCGSNGDTYQNECFLRRAACKHQKEITVIARGPCYSDNGSGSGEGEEEGSGAEVHRKHSKCGPCKYKAECDEDAENVGCVCNIDCSGYSFNPVCASDGSSYNNPCFVREASCIKQEQIDIRHLGHCTDTDDTSLLGKKDDGLQYRPDVKDASDQREDVYIGNHMPCPENLNGYCIHGKCEFIYSTQKASCRCESGYTGQHCEKTDFSILYVVPSRQKLTHV |
| 预测分子量 | 38.5 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TR1(假设为TGF-β受体1或相关蛋白)重组蛋白的示例参考文献(文献为虚构示例，实际引用请查询真实数据库)：
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1. **《Expression and purification of recombinant human TR1 for functional studies》**
*作者：Smith A, et al.*
**摘要**：研究通过大肠杆菌表达系统优化了人源TR1重组蛋白的克隆与纯化，验证了其与配体TGF-β的结合活性，为后续信号通路研究提供工具。
2. **《Structural analysis of TR1 extracellular domain reveals key motifs in ligand recognition》**
*作者：Chen L, Wang H.*
**摘要**：通过X射线晶体学解析TR1胞外结构域的三维结构，揭示了其与TGF-β相互作用的特异性氨基酸残基，为靶向药物设计提供结构基础。
3. **《TR1 knockdown exacerbates fibrosis in a murine liver injury model》**
*作者：Kimura T, et al.*
**摘要**：利用重组TR1蛋白干预小鼠肝纤维化模型，证明TR1通过调控Smad磷酸化抑制纤维化进程，提示其潜在治疗价值。
4. **《High-yield production of bioactive TR1 in mammalian cell culture》**
*作者：Rodriguez M, et al.*
**摘要**：对比不同哺乳动物表达系统(如CHO细胞)中TR1的糖基化修饰差异，证实哺乳细胞源重组TR1具有更接近天然蛋白的生物活性。
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注：以上文献为模拟内容，实际研究中请通过PubMed、Google Scholar等平台检索真实文献(关键词如“TGFBR1 recombinant protein”或“Thioredoxin Reductase 1 expression”)。
**Background of TR1 Recombinant Protein**
TR1 (TGF-β Receptor Type 1), also known as activin receptor-like kinase 5 (ALK5), is a key component of the transforming growth factor-beta (TGF-β) signaling pathway. This transmembrane serine/threonine kinase receptor plays a central role in mediating cellular responses to TGF-β ligands, including regulation of cell proliferation, differentiation, apoptosis, and extracellular matrix production. Dysregulation of TGF-β signaling is implicated in diverse pathologies, such as fibrosis, cancer metastasis, and autoimmune disorders, making TR1 a critical therapeutic target.
Recombinant TR1 protein is engineered through biotechnological methods, often expressed in mammalian or insect cell systems to ensure proper post-translational modifications and functionality. It is commonly produced as a soluble extracellular domain (ECD) or fused with Fc tags to enhance stability and bioavailability. These recombinant forms are designed to mimic or antagonize native receptor-ligand interactions, serving as decoy receptors to sequester excess TGF-β ligands, thereby modulating downstream signaling.
In research, TR1 recombinant protein is widely used to study TGF-β pathway mechanisms, screen inhibitors, or develop targeted therapies. For instance, soluble TR1-Fc fusion proteins have shown promise in preclinical models of fibrosis and cancer by blocking TGF-β-induced Smad phosphorylation and epithelial-mesenchymal transition (EMT). Additionally, TR1-targeting monoclonal antibodies and kinase inhibitors are under investigation to counteract pathological TGF-β activation.
Despite its therapeutic potential, challenges remain, including optimizing receptor specificity to minimize off-target effects and improving delivery strategies. Ongoing studies aim to refine TR1-based biologics for clinical translation, highlighting its significance in bridging fundamental research and drug development for TGF-β-driven diseases.
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