| 纯度 | ＞80%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Smad3 |
| Uniprot No | P84022 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-425aa |
| 氨基酸序列 | MSSILPFTPPIVKRLLGWKKGEQNGQEEKWCEKAVKSLVKKLKKTGQLDE LEKAITTQNV NTKCITIPRSLDGRLQVSHRKGLPHVIYCRLWRWPDLH SHHELRAMELCEFAFNMKKDEV CVNPYHYQRVETPVLPPVLVPRHTEI PAEFPPLDDYSHSIPENTNFPAGIEPQSNIPETP PPGYLSEDGETSDH QMNHSMDAGSPNLSPNPMSPAHNNLDLQPVTYCEPAFWCSISYYELNQRV GETFHASQPSMTVDGFTDPSNSERFCLGLLSNVNRNAAVELTRRHIGRGV RLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFN NQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPC WIELHLNGPLQWLDKVLTQMGSPSIRCSSVS |
| 预测分子量 | 77 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3篇关于Smad3重组蛋白的代表性文献(标题、作者及摘要概括)：
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1. **文献名称**: *"MADR2. a mediator of TGF-β signals, is phosphorylated by the TGF-β receptor"*
**作者**: Souchelnytskyi S, et al.
**摘要**: 研究利用重组Smad3蛋白(MADR2)在体外验证其被TGF-β受体直接磷酸化的机制，揭示了Smad3的C端SSXS基序是磷酸化关键位点，并证实磷酸化后触发其核转位。
2. **文献名称**: *"Crystal structure of a Smad MH1 domain bound to DNA: insights into DNA binding in TGF-β signaling"*
**作者**: Shi Y, et al.
**摘要**: 通过表达纯化重组Smad3的MH1结构域，解析其与DNA复合物的晶体结构，阐明Smad3如何特异性识别TGF-β响应基因的DNA结合序列，为信号转导机制提供结构基础。
3. **文献名称**: *"Cooperative binding of Smad proteins to overlapping DNA motifs in TGF-β responsive promoters"*
**作者**: Zawel L, et al.
**摘要**: 利用重组Smad3/Smad4蛋白进行体外DNA结合实验，证明两者通过协同作用结合靶基因启动子区域，揭示了Smad复合物调控基因表达的分子机制。
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以上文献均涉及重组Smad3蛋白的制备及其在信号转导、结构解析或功能验证中的应用，涵盖磷酸化、DNA结合及复合物形成等关键生物学过程。
**Background of Smad3 Recombinant Protein**
Smad3 is a critical intracellular signaling mediator within the transforming growth factor-beta (TGF-β) superfamily pathway, which regulates diverse cellular processes, including proliferation, differentiation, apoptosis, and extracellular matrix production. As a member of the receptor-regulated Smad (R-Smad) family, Smad3 is directly phosphorylated by activated TGF-β type I receptors upon ligand binding. This phosphorylation triggers its dissociation from the receptor, subsequent binding to Smad4 (a common mediator Smad), and translocation into the nucleus. There, the Smad3/Smad4 complex modulates the transcription of target genes by interacting with specific DNA sequences and co-regulators.
Recombinant Smad3 protein is engineered *in vitro* using expression systems (e.g., *E. coli*, mammalian, or insect cells*) to produce a purified, functional form of the protein for research and therapeutic applications. The protein typically retains key structural domains: the N-terminal MH1 domain for DNA binding and the C-terminal MH2 domain for protein interactions and transcriptional activation. Post-translational modifications, such as phosphorylation, can be mimicked or analyzed to study regulatory mechanisms.
Smad3 dysregulation is implicated in fibrosis, cancer, and immune disorders. For instance, hyperactive Smad3 signaling promotes fibrosis by enhancing collagen deposition, while its loss or mutation may contribute to tumor progression. Recombinant Smad3 enables researchers to dissect these mechanisms, screen TGF-β pathway inhibitors, or develop targeted therapies. It is also used in *in vitro* assays (e.g., kinase activity, DNA-binding studies) and disease modeling.
Advances in protein engineering have improved Smad3 recombinant variants, including tagged versions (e.g., His-, GST-tags) for easier purification and detection. Functional validation via techniques like electrophoretic mobility shift assays (EMSAs) or luciferase reporter systems ensures its biological activity. Overall, Smad3 recombinant protein serves as a vital tool for unraveling TGF-β signaling complexities and exploring therapeutic interventions in Smad3-associated diseases.
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