
抗人 PYGO1 抗体对
01AB03004
Pygopus family PHD finger 1 (PYGO1) is a nuclear protein that contains a PHD zinc finger domain at its C terminus, which mediates protein-protein interactions rather than DNA binding. PYGO1 plays a crucial role in chromatin remodeling by associating with transcription co-factors such as histone 3 and BCL9/9L, forming complexes that regulate gene expression, particularly in the Wnt/β-catenin signaling pathway. Its PHD domain participates in dimerization, essential for interaction with BCL9 proteins and transcriptional activation. PYGO1 is evolutionarily conserved and acts downstream or at the level of TCF/β-catenin in Wnt signaling, important for embryonic development and tissue-specific transcription regulation. Dysfunction or altered regulation of PYGO1 has been implicated in carcinogenesis, with evidence showing it as a core effector in cancer-related Wnt pathway activation.
| 规格 | 起售价 |
|---|---|
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技术参数
- 靶点基因名
- PYGO1
- 蛋白别名
- pygopus family PHD finger 1; PYGO1
- UniProt
- Q9Y3Y4
- 物种
- Human
产品详情
- 靶点名称
- PYGO1
- 蛋白名称
- pygopus family PHD finger 1
- 蛋白别名
- Pygopus homolog 1
- 靶点基因名
- PYGO1
- UniProt
- Q9Y3Y4
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Pygopus family PHD finger 1 (PYGO1) is a nuclear protein that contains a PHD zinc finger domain at its C terminus, which mediates protein-protein interactions rather than DNA binding. PYGO1 plays a crucial role in chromatin remodeling by associating with transcription co-factors such as histone 3 and BCL9/9L, forming complexes that regulate gene expression, particularly in the Wnt/β-catenin signaling pathway. Its PHD domain participates in dimerization, essential for interaction with BCL9 proteins and transcriptional activation. PYGO1 is evolutionarily conserved and acts downstream or at the level of TCF/β-catenin in Wnt signaling, important for embryonic development and tissue-specific transcription regulation. Dysfunction or altered regulation of PYGO1 has been implicated in carcinogenesis, with evidence showing it as a core effector in cancer-related Wnt pathway activation.