抗人 SMAD1 抗体对
01AB01591
SMAD family member 1 (SMAD1) is a receptor-regulated SMAD (R-SMAD) that functions as a transcriptional modulator within the bone morphogenetic protein (BMP) signaling pathway. Upon BMP ligand binding, SMAD1 is C-terminally phosphorylated by type I BMP receptors, enabling it to form heteromeric complexes with SMAD4. This complex translocates to the nucleus to bind Smad binding elements and regulate the transcription of genes involved in embryonic development, cell differentiation, and tissue homeostasis. Structurally, SMAD1 contains MH1 and MH2 domains for DNA binding and protein interactions, respectively. Its activity is negatively regulated by E3 ubiquitin ligases such as SMURF1 and SMURF2, which target it for proteasomal degradation. Pathologically, dysregulated SMAD1 signaling is implicated in disorders such as Hermansky-Pudlak syndrome 2 and fibrodysplasia ossificans progressiva.
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技术参数
- 靶点基因名
- SMAD1
- 基因别名
- BSP1; MADH1; MADR1
- 蛋白别名
- SMAD family member 1; SMAD1
- UniProt
- Q15797
- 物种
- Human
产品详情
- 靶点名称
- SMAD1
- 蛋白名称
- SMAD family member 1
- 蛋白别名
- Mothers against decapentaplegic homolog 1; MAD homolog 1; Mothers against DPP homolog 1; JV4-1; Mad-related protein 1; SMAD family member 1; SMAD 1; Smad1; hSMAD1; Transforming growth factor-beta-signaling protein 1; BSP-1
- 靶点基因名
- SMAD1
- 基因别名
- BSP1; MADH1; MADR1
- UniProt
- Q15797
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
SMAD family member 1 (SMAD1) is a receptor-regulated SMAD (R-SMAD) that functions as a transcriptional modulator within the bone morphogenetic protein (BMP) signaling pathway. Upon BMP ligand binding, SMAD1 is C-terminally phosphorylated by type I BMP receptors, enabling it to form heteromeric complexes with SMAD4. This complex translocates to the nucleus to bind Smad binding elements and regulate the transcription of genes involved in embryonic development, cell differentiation, and tissue homeostasis. Structurally, SMAD1 contains MH1 and MH2 domains for DNA binding and protein interactions, respectively. Its activity is negatively regulated by E3 ubiquitin ligases such as SMURF1 and SMURF2, which target it for proteasomal degradation. Pathologically, dysregulated SMAD1 signaling is implicated in disorders such as Hermansky-Pudlak syndrome 2 and fibrodysplasia ossificans progressiva.