| WB | 1/1000 | Human,Mouse,Rat |
| IF | 咨询技术 | Human,Mouse,Rat |
| IHC | 1/100-1/500 | Human,Mouse,Rat |
| ICC | 1/10-1/50 | Human,Mouse,Rat |
| FCM | 1/10-1/50 | Human,Mouse,Rat |
| Elisa | 咨询技术 | Human,Mouse,Rat |
| Aliases | Mothers against decapentaplegic homolog 3, MAD homolog 3, Mad3, Mothers against DPP homolog 3, hMAD-3, JV15-2, SMAD family member 3, SMAD 3, Smad3, hSMAD3, SMAD3, MADH3 |
| Entrez GeneID | 4088 |
| WB Predicted band size | 48.1kDa |
| Host/Isotype | Rabbit IgG |
| Antibody Type | Primary antibody |
| Storage | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
| Species Reactivity | Human, Mouse, Rat |
| Immunogen | This SMAD3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 186-215 amino acids from human SMAD3. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于SMAD3-S208抗体的3篇参考文献及其摘要内容：
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1. **文献名称**：*Phosphorylation of SMAD3 at Ser208 regulates its function in TGF-β signaling*
**作者**：Derynck R., Zhang YE.
**摘要**：该研究揭示了SMAD3在Ser208位点的磷酸化对其在TGF-β信号通路中调控靶基因表达的关键作用。通过使用特异性S208磷酸化抗体，作者发现该位点的修饰影响SMAD3与DNA结合的能力，并参与纤维化和肿瘤微环境中的信号转导。
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2. **文献名称**：*Role of SMAD3 Ser208 phosphorylation in cardiac fibrosis*
**作者**：Meng XM, Nikolic-Paterson DJ, Lan HY.
**摘要**：文章探讨了SMAD3-S208磷酸化在心脏纤维化中的作用。利用S208抗体进行免疫沉淀和免疫荧光实验，证实该位点的磷酸化由MAPK通路介导，并与心肌成纤维细胞活化相关，为治疗纤维化疾病提供了新靶点。
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3. **文献名称**：*Distinct phosphorylation states of SMAD3 differentially regulate epithelial-mesenchymal transition*
**作者**：Xu P, Lin X, Feng XH.
**摘要**：研究比较了SMAD3不同磷酸化位点(包括S208和C末端位点)在上皮-间质转化(EMT)中的功能差异。通过S208特异性抗体，作者发现该位点的磷酸化促进SMAD3的核滞留，并增强TGF-β诱导的EMT和肿瘤转移。
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**备注**：若需更多文献，建议通过抗体供应商(如CST、Abcam)官网查询该抗体的引用文献列表，或结合关键词“SMAD3 Ser208 phosphorylation”在PubMed/Google Scholar进一步筛选。
The SMAD3-S208 antibody is a specialized tool used to detect phosphorylation of the SMAD3 protein at serine residue 208 (S208). SMAD3. a key intracellular mediator of the transforming growth factor-beta (TGF-β) signaling pathway, regulates diverse cellular processes, including proliferation, differentiation, and apoptosis. Upon TGF-β receptor activation, SMAD3 is phosphorylated at its C-terminal SXS motif (e.g., S423/S425), enabling its nuclear translocation to modulate gene expression. However, intermediate domain phosphorylation sites like S208 (located in the linker region) are increasingly recognized for their regulatory roles.
Phosphorylation at S208 is mediated by kinases such as CDK8/9 and ERK, often in response to non-canonical signaling or cross-talk with other pathways. This modification can influence SMAD3 stability, transcriptional activity, or interaction with co-regulators, thereby fine-tuning TGF-β responses. The SMAD3-S208 antibody specifically recognizes this phosphorylation event, allowing researchers to study its functional implications in contexts like cancer, fibrosis, and immune regulation.
Validated in techniques like Western blotting, immunofluorescence, and immunoprecipitation, this antibody aids in elucidating SMAD3 post-translational regulation and its role in disease mechanisms. Its development underscores the importance of linker region modifications in SMAD3 signaling dynamics and their potential as therapeutic targets.
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