人 THOP1 抗体对
01AB03696
Thimet oligopeptidase (THOP1) is a metallopeptidase that plays a significant role in the degradation of various bioactive peptides, including neuropeptides and hormones. This enzyme is characterized by its ability to cleave peptide bonds, particularly those involving proline residues, and is involved in modulating physiological processes such as neurotransmission and immune response. THOP1 is primarily located in the cytosol and is associated with intracellular signaling pathways. Dysregulation of THOP1 has been linked to several diseases, including neurodegenerative disorders like Alzheimer's disease, where altered peptide processing may contribute to the accumulation of toxic aggregates. Additionally, THOP1 has been implicated in cancer biology; its expression levels can influence tumor progression and metastasis by affecting the availability of signaling peptides.
| 规格 | 起售价 |
|---|---|
| 登录后可查看 | |
技术参数
- 靶点基因名
- THOP1
- 蛋白别名
- thimet oligopeptidase 1; THOP1
- UniProt
- P52888
- 物种
- Human
产品详情
- 靶点名称
- THOP1
- 蛋白名称
- thimet oligopeptidase 1
- 蛋白别名
- Thimet oligopeptidase; Endopeptidase 24.15; MP78
- 靶点基因名
- THOP1
- UniProt
- P52888
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Thimet oligopeptidase (THOP1) is a metallopeptidase that plays a significant role in the degradation of various bioactive peptides, including neuropeptides and hormones. This enzyme is characterized by its ability to cleave peptide bonds, particularly those involving proline residues, and is involved in modulating physiological processes such as neurotransmission and immune response. THOP1 is primarily located in the cytosol and is associated with intracellular signaling pathways. Dysregulation of THOP1 has been linked to several diseases, including neurodegenerative disorders like Alzheimer's disease, where altered peptide processing may contribute to the accumulation of toxic aggregates. Additionally, THOP1 has been implicated in cancer biology; its expression levels can influence tumor progression and metastasis by affecting the availability of signaling peptides.