| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TGFBR2 |
| Uniprot No | P37173 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 23-166aa |
| 氨基酸序列 | TIPPHVQKSVNNDMIVTDNNGAVKFPQLCKFCDVRFSTCDNQKSCMSNCSITSICEKPQEVCVAVWRKNDENITLETVCHDPKLPYHDFILEDAASPKCIMKEKKKPGETFFMCSCSSDECNDNIIFSEEYNTSNPDLLLVIFQ |
| 预测分子量 | 23.8 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TGFBR2重组蛋白的3篇代表性文献及其摘要内容：
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1. **文献名称**: *"Structure and functional analysis of the TGF-β receptor TβRII: Binding of TGF-β3"*
**作者**: Hart PJ 等
**摘要**: 该研究解析了TGFBR2胞外结构域与TGF-β3复合物的晶体结构，揭示了受体与配体结合的关键位点，并发现其结合模式与TGF-β1不同，为靶向TGF-β信号通路的药物设计提供了结构基础。
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2. **文献名称**: *"Expression and purification of recombinant human TGFBR2 kinase domain for functional studies"*
**作者**: Zhang Y 等
**摘要**: 文章报道了人源TGFBR2激酶结构域的重组表达与纯化方法，通过体外激酶实验验证其活性，并筛选了小分子抑制剂，为研究TGF-β信号传导机制及开发相关抑制剂提供了工具。
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3. **文献名称**: *"TGFBR2 mutations in human cancers: Functional impact and therapeutic implications"*
**作者**: Grady WM 等
**摘要**: 该综述总结了TGFBR2在结直肠癌等肿瘤中的突变谱，分析了突变导致受体功能丧失的机制，并探讨了通过重组蛋白模型研究突变对TGF-β信号抑制的作用，提出靶向策略的潜在方向。
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如需更多文献或具体研究方向(如重组蛋白应用、结构生物学等)，可进一步补充说明!
TGFBR2 (transforming growth factor-beta receptor type II) is a transmembrane serine/threonine kinase receptor that plays a central role in the TGF-β signaling pathway. This receptor binds TGF-β ligands (including TGF-β1. TGF-β2. and TGF-β3) and forms a heteromeric complex with TGFBR1. initiating intracellular signaling cascades involved in cell proliferation, differentiation, apoptosis, and extracellular matrix production. Dysregulation of TGFBR2 is linked to various diseases, including cancer, fibrosis, and cardiovascular disorders.
Recombinant TGFBR2 proteins are engineered versions of the receptor, typically produced in mammalian or insect expression systems to ensure proper post-translational modifications. These proteins often include the extracellular ligand-binding domain (amino acids 1-159) or full-length constructs for functional studies. The extracellular domain mediates ligand recognition, while the intracellular kinase domain transmits signals via phosphorylation of downstream SMAD proteins.
Researchers utilize recombinant TGFBR2 to investigate TGF-β pathway mechanisms, screen for therapeutic inhibitors, and study receptor-ligand interactions. In cancer biology, loss-of-function TGFBR2 mutations are associated with resistance to TGF-β-mediated growth inhibition, making the receptor a potential biomarker and therapeutic target. Conversely, in fibrotic diseases, enhanced TGFBR2 signaling drives pathological tissue remodeling.
Clinical applications of recombinant TGFBR2 include developing decoy receptors to neutralize excessive TGF-β activity in fibrosis and metastatic cancers. Notably, soluble TGFBR2-Fc fusion proteins have shown promise in preclinical models for blocking TGF-β signaling. In genetic disorders like Marfan syndrome, recombinant TGFBR2 helps study pathway dysregulation caused by FBN1 mutations. The protein's versatility as both a research tool and therapeutic candidate continues to expand our understanding of TGF-β biology and its clinical implications.
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