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| 纯度 | >98%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TGFB1 |
| Uniprot No | P01137 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 279-390aa |
| 氨基酸序列 | ALDTNYCFSS TEKNCCVRQL YIDFRKDLGW KWIHEPKGYH ANFCLGPCPY IWSLDTQYSK VLALYNQHNP GASAAPCCVP QALEPLPIVY YVGRKPKVEQ LSNMIVRSCK CS |
| 预测分子量 | 25 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TGFB1重组蛋白的3-4篇参考文献的简要总结：
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1. **文献名称**: *"Expression and characterization of recombinant human transforming growth factor beta-1 (TGF-β1) in prokaryotic and eukaryotic systems*"
**作者**: Derynck R, et al.
**摘要**: 该研究描述了在大肠杆菌(原核)和哺乳动物细胞(真核)系统中表达重组人TGF-β1的方法，比较了两者的蛋白活性，证明哺乳动物系统产生的TGF-β1具有更高的生物活性，适用于细胞功能研究。
2. **文献名称**: *"Latent transforming growth factor-beta (TGF-β) binding proteins: extracellular matrix association and roles in TGF-β activation*"
**作者**: Saharinen J, et al.
**摘要**: 研究了重组TGF-β1与其潜在结合蛋白(LTBPs)的相互作用，阐明了细胞外基质对TGF-β1活化的调控机制，为重组蛋白在组织修复研究中的应用提供依据。
3. **文献名称**: *"Recombinant TGF-β1 induces extracellular matrix deposition and fibrosis in vitro*"
**作者**: Leask A, et al.
**摘要**: 通过体外实验证明，重组TGF-β1可显著促进成纤维细胞的胶原合成和纤维化相关基因表达，支持其在纤维化疾病模型(如肺纤维化、肝纤维化)中的病理机制研究。
4. **文献名称**: *"Optimization of TGF-β1 purification from recombinant mammalian cell culture using heparin affinity chromatography*"
**作者**: Gentry LE, et al.
**摘要**: 提出了一种基于肝素亲和层析的高效纯化重组TGF-β1的方法，显著提高了蛋白纯度和产量，适用于大规模制备治疗或实验用途的TGF-β1.
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这些文献涵盖了重组TGFB1的表达系统开发、功能研究及生物医学应用，为相关研究提供了技术参考和理论支持。
Transforming growth factor beta 1 (TGFB1) is a multifunctional cytokine belonging to the TGF-β superfamily, first identified in the 1980s for its ability to induce anchorage-independent growth in fibroblasts. It plays pivotal roles in regulating cell proliferation, differentiation, apoptosis, immune response, and extracellular matrix remodeling. Mature TGFB1 is a 25 kDa homodimeric protein derived from proteolytic cleavage of a latent precursor. Its signaling occurs through serine/threonine kinase receptors (TGFBR1/2), activating SMAD-dependent and non-canonical pathways (e.g., MAPK, PI3K) to mediate context-dependent cellular responses.
Recombinant TGFB1 is produced using mammalian expression systems (e.g., CHO or HEK293 cells) to ensure proper post-translational modifications, particularly the formation of disulfide-linked dimers critical for bioactivity. The protein is typically purified via chromatography and rigorously tested for endotoxin levels and functional consistency using cell-based assays like luciferase reporter systems or SMAD phosphorylation analyses.
In research, recombinant TGFB1 is widely used to study mechanisms underlying fibrosis, cancer progression (dual roles in tumor suppression and metastasis), immune tolerance, and wound healing. It serves as a therapeutic target in clinical trials for diseases ranging from idiopathic pulmonary fibrosis to advanced cancers, with inhibitors like monoclonal antibodies and kinase modulators in development. However, its pleiotropic nature – acting as both a tumor suppressor in early-stage cancers and a promoter of invasion in advanced malignancies – underscores the complexity of harnessing TGFB1 signaling therapeutically. Recent advances in structural biology and conditional knockout models have refined understanding of its spatiotemporal regulation, driving innovation in tissue-specific drug delivery strategies.
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