人 METAP1 抗体对
01AB01225
Methionyl aminopeptidase 1 (METAP1) is a crucial enzyme belonging to the peptidase M24A family that catalyzes the removal of the N-terminal methionine from nascent proteins, particularly when the second amino acid is small and uncharged (such as Ala, Cys, Gly, Pro, Ser, Thr, or Val). This processing is essential for proper protein maturation and function, and METAP1’s activity is vital for normal cell cycle progression, especially during the G2/M phase transition. Structurally, METAP1 is a single-chain polypeptide with a molecular weight of approximately 38–50 kDa, featuring an active site with two adjacent divalent metal ions that are critical for its catalytic function. Functionally, METAP1 is highly conserved across species and can complement the loss of its yeast counterpart, highlighting its fundamental biological role. In disease contexts, inhibition or knockdown of METAP1 disrupts cell cycle progression, induces apoptosis in cancer cell lines, and has been proposed as a promising target for anticancer drug development due to its role in regulating cell division and survival.
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技术参数
- 靶点基因名
- METAP1
- 基因别名
- KIAA0094
- 蛋白别名
- methionyl aminopeptidase 1; METAP1
- UniProt
- P53582
- 物种
- Human
产品详情
- 靶点名称
- METAP1
- 蛋白名称
- methionyl aminopeptidase 1
- 蛋白别名
- Methionine aminopeptidase 1; MAP 1; MetAP 1; Peptidase M 1
- 靶点基因名
- METAP1
- 基因别名
- KIAA0094
- UniProt
- P53582
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Methionyl aminopeptidase 1 (METAP1) is a crucial enzyme belonging to the peptidase M24A family that catalyzes the removal of the N-terminal methionine from nascent proteins, particularly when the second amino acid is small and uncharged (such as Ala, Cys, Gly, Pro, Ser, Thr, or Val). This processing is essential for proper protein maturation and function, and METAP1’s activity is vital for normal cell cycle progression, especially during the G2/M phase transition. Structurally, METAP1 is a single-chain polypeptide with a molecular weight of approximately 38–50 kDa, featuring an active site with two adjacent divalent metal ions that are critical for its catalytic function. Functionally, METAP1 is highly conserved across species and can complement the loss of its yeast counterpart, highlighting its fundamental biological role. In disease contexts, inhibition or knockdown of METAP1 disrupts cell cycle progression, induces apoptosis in cancer cell lines, and has been proposed as a promising target for anticancer drug development due to its role in regulating cell division and survival.