| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Smad4 |
| Uniprot No | Q9NPI6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-582aa |
| 氨基酸序列 | MEALSRAGQEMSLAALKQHDPYITSIADLTGQVALYTFCPKANQWEKTDIEGTLFVYRRSASPYHGFTIVNRLNMHNLVEPVNKDLEFQLHEPFLLYRNASLSIYSIWFYDKNDCHRIAKLMADVVEEETRRSQQAARDKQSPSQANGCSDHRPIDILEMLSRAKDEYERNQMGDSNISSPGLQPSTQLSNLGSTETLEEMPSGSQDKSAPSGHKHLTVEELFGTSLPKEQPAVVGLDSEEMERLPGDASQKEPNSFLPFPFEQLGGAPQSETLGVPSAAHHSVQPEITTPVLITPASITQSNEKHAPTYTIPLSPVLSPTLPAEAPTAQVPPSLPRNSTMMQAVKTTPRQRSPLLNQPVPELSHASLIANQSPFRAPLNVTNTAGTSLPSVDLLQKLRLTPQHDQIQTQPLGKGAMVASFSPAAGQLATPESFIEPPSKTAAARVAASASLSNMVLAPLQSMQQNQDPEVFVQPKVLSSAIQVAGAPLVTATTTAVSSVLLAPSVFQQTVTRSSDLERKASSPSPLTIGTPESQRKPSIILSKSQLQDTLIHLIKNDSSFLSTLHEVYLQVLTKNKDNHNL |
| 预测分子量 | 67.3kDa |
| 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篇与Smad4重组蛋白相关的文献示例(内容为模拟概括，建议核实原文)：
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1. **文献名称**: "Recombinant Smad4: Purification and Functional Analysis in TGF-β Signaling"
**作者**: Derynck R, et al.
**摘要**: 研究通过大肠杆菌表达系统制备重组Smad4蛋白，验证其与Smad2/3及DNA的结合能力，揭示其在TGF-β信号通路中的核心作用。
2. **文献名称**: "Crystal Structure of Smad4 MH2 Domain Complexed with Smad2"
**作者**: Shi Y, et al.
**摘要**: 解析Smad4重组蛋白的MH2结构域晶体结构，阐明其与磷酸化Smad2的互作机制，为TGF-β信号转导提供结构生物学依据。
3. **文献名称**: "Loss of Smad4 Promotes Metastasis in Colorectal Cancer"
**作者**: Massagué J, et al.
**摘要**: 利用重组Smad4蛋白进行功能回补实验，证明Smad4缺失通过破坏TGF-β抑癌通路驱动结直肠癌转移，提示其肿瘤抑制作用。
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注：以上为示例性内容，实际文献需通过PubMed/Google Scholar检索关键词(如"Recombinant Smad4 protein"、"Smad4 purification")获取准确信息。
**Background of Smad4 Recombinant Protein**
Smad4. a pivotal mediator in the transforming growth factor-beta (TGF-β) signaling pathway, plays a central role in regulating cellular processes such as proliferation, differentiation, apoptosis, and immune responses. As a member of the Smad family, Smad4 functions as a common-mediator Smad (co-Smad), partnering with receptor-activated Smads (R-Smads) to transduce signals from TGF-β superfamily receptors to the nucleus. Upon ligand binding, TGF-β receptors phosphorylate R-Smads, which then form complexes with Smad4. These complexes translocate to the nucleus, where they regulate the transcription of target genes by interacting with DNA and co-activators or co-repressors.
Recombinant Smad4 protein is engineered through genetic cloning and expression in heterologous systems (e.g., *E. coli*, insect, or mammalian cells*)*, enabling large-scale production for research and therapeutic applications. Its recombinant form retains functional domains critical for signaling, including the N-terminal Mad homology 1 (MH1) domain for DNA binding and the C-terminal MH2 domain for protein interactions. Purified Smad4 is widely used to study TGF-β pathway mechanisms, protein-protein/DNA interactions, and dysregulation in diseases like cancer, fibrosis, and immune disorders.
Notably, Smad4 mutations or deletions are linked to pancreatic, colorectal, and other cancers, where disrupted TGF-β signaling promotes tumor progression. Recombinant Smad4 facilitates drug discovery by serving as a tool to screen compounds targeting TGF-β pathways or restore Smad4 function in preclinical models. Additionally, it aids in structural studies to elucidate Smad4’s molecular interactions, advancing the design of pathway-specific therapeutics. Tags (e.g., His, GST) are often fused to the protein for simplified purification and detection, ensuring experimental versatility. Overall, Smad4 recombinant protein remains indispensable for decoding TGF-β biology and developing precision medicine strategies.
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