抗人 CPM 抗体对
01AB00783
Carboxypeptidase M (CPM) is a membrane-bound zinc metalloprotease that specifically removes C-terminal basic residues (arginine or lysine) from peptides and proteins. It is widely distributed in human tissues and plays important roles in regulating peptide hormone and growth factor activity at the cell surface. CPM consists of a 295-residue N-terminal catalytic domain and an 86-residue C-terminal domain, with a unique 25-residue C-terminal extension for GPI-anchor attachment. The enzyme is involved in various physiological processes, including inflammation, angiogenesis, and cell differentiation. CPM has been associated with several pathological conditions, such as renal cell carcinoma, where its expression is lost in tumor cells but abundant in tumor-associated foam cells. Additionally, CPM has been linked to silicosis susceptibility, with the rs12812500 variant potentially affecting CPM expression and increasing disease risk.
| 规格 | 起售价 |
|---|---|
| 登录后可查看 | |
技术参数
- 靶点基因名
- CPM
- 蛋白别名
- carboxypeptidase M; CPM
- UniProt
- P14384
- 物种
- Human
产品详情
- 靶点名称
- CPM
- 蛋白名称
- carboxypeptidase M
- 蛋白别名
- Carboxypeptidase M; CPM
- 靶点基因名
- CPM
- UniProt
- P14384
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Carboxypeptidase M (CPM) is a membrane-bound zinc metalloprotease that specifically removes C-terminal basic residues (arginine or lysine) from peptides and proteins. It is widely distributed in human tissues and plays important roles in regulating peptide hormone and growth factor activity at the cell surface. CPM consists of a 295-residue N-terminal catalytic domain and an 86-residue C-terminal domain, with a unique 25-residue C-terminal extension for GPI-anchor attachment. The enzyme is involved in various physiological processes, including inflammation, angiogenesis, and cell differentiation. CPM has been associated with several pathological conditions, such as renal cell carcinoma, where its expression is lost in tumor cells but abundant in tumor-associated foam cells. Additionally, CPM has been linked to silicosis susceptibility, with the rs12812500 variant potentially affecting CPM expression and increasing disease risk.