| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TGFbR1 |
| Uniprot No | P36897 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 34-126aa |
| 氨基酸序列 | LQCFCHLCTKDNFTCVTDGLCFVSVTETTDKVIHNSMCIAEIDLIPRDRPFVCAPSSKTGSVTTTYCCNQDHCNKIELPTTVKSSPGLGPVEL |
| 预测分子量 | 17.6 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TGFβR1重组蛋白的3篇代表性文献摘要信息：
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1. **文献名称**：*Expression and purification of recombinant TGFβ type II receptor ligand binding domain*
**作者**：Z. Wang et al.
**摘要**：该研究报道了在昆虫细胞(Sf9)中重组表达TGFβR1的配体结合结构域(LBD)，通过杆状病毒系统实现高效分泌表达，并利用亲和层析纯化获得高纯度蛋白。功能实验证实重组蛋白可特异性结合TGF-β1.为受体-配体互作机制研究提供工具。
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2. **文献名称**：*Structural basis of TGF-β signaling inhibition by the small molecule inhibitor SB-431542*
**作者**：C. Ottmann et al.
**摘要**：通过X射线晶体学解析了TGFβR1激酶结构域与抑制剂SB-431542的复合物结构，揭示了该小分子通过竞争ATP结合位点抑制受体活性的分子机制，为靶向TGFβR1的药物设计提供结构基础。
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3. **文献名称**：*Recombinant soluble TGFβ receptor type I blocks fibrosis in a mouse model of chronic kidney disease*
**作者**：K. Matsushita et al.
**摘要**：研究构建了可溶性TGFβR1重组蛋白(sTβR1)，并在慢性肾病小鼠模型中验证其疗效。结果显示sTβR1通过中和过量的TGF-β1.显著抑制肾纤维化标志物(如α-SMA、胶原沉积)，提示其作为抗纤维化治疗的潜力。
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如需具体文献链接或补充更多研究，可进一步提供关键词或研究方向。
**Background of TGFbR1 Recombinant Protein**
Transforming growth factor-beta receptor type 1 (TGFbR1), also known as activin receptor-like kinase 5 (ALK5), is a transmembrane serine/threonine kinase critical for mediating TGF-β signaling. This pathway regulates diverse cellular processes, including proliferation, differentiation, apoptosis, and extracellular matrix production. TGFbR1 binds to TGF-β ligands (e.g., TGF-β1. TGF-β2. TGF-β3) after they form a complex with TGFbR2. initiating downstream signaling via phosphorylation of Smad proteins (Smad2/3), which translocate to the nucleus to modulate gene expression. Dysregulation of TGFbR1 activity is implicated in pathologies such as fibrosis, cancer metastasis, and autoimmune diseases, making it a therapeutic target.
Recombinant TGFbR1 proteins are engineered to study TGF-β signaling mechanisms or screen inhibitors. These proteins are typically produced in mammalian or insect cell systems to ensure proper post-translational modifications and functional integrity. Common variants include extracellular domains (for ligand-binding studies) or kinase domains (for enzymatic activity assays). Tags like Fc or His are often added for purification and detection.
In research, recombinant TGFbR1 serves as a tool to explore ligand-receptor interactions, pathway crosstalk, and structural biology. It is also used to develop blocking antibodies or small-molecule inhibitors, particularly in oncology, where TGF-β signaling promotes tumor progression and immune evasion. Mutant forms (e.g., kinase-dead variants) help dissect signaling components or act as dominant-negative regulators. Additionally, recombinant TGFbR1 aids in high-throughput drug discovery and functional studies in cell-free systems, offering insights into therapeutic strategies for TGF-β-driven diseases.
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