
人 PGP 抗体对
01AB02248
Phosphoglycolate phosphatase (PGP) is a conserved cytosolic hydrolase of the haloacid dehalogenase family that functions as a metabolic proofreading enzyme. It specifically dephosphorylates 2-phosphoglycolate and related damage metabolites, such as 2-phospho-L-lactate, which are generated during oxidative DNA damage repair. By clearing these metabolites, PGP prevents the inhibition of key glycolytic enzymes, including triosephosphate isomerase and phosphofructokinase, thereby maintaining metabolic flux. PGP activity is essential for embryonic development and sustained cell proliferation, as it couples the products of DNA repair to intermediary metabolism. Its critical role in cellular survival is further evidenced by its necessity for parasite viability in Plasmodium species, suggesting its importance across diverse biological systems.
| 规格 | 起售价 |
|---|---|
| 登录后可查看 | |
技术参数
- 靶点基因名
- PGP
- 蛋白别名
- phosphoglycolate phosphatase; PGP
- UniProt
- A6NDG6
- 物种
- Human
产品详情
- 靶点名称
- PGP
- 蛋白名称
- phosphoglycolate phosphatase
- 蛋白别名
- Glycerol-3-phosphate phosphatase; G3PP; Aspartate-based ubiquitous Mg(2+)-dependent phosphatase; AUM; Phosphoglycolate phosphatase; PGP
- 靶点基因名
- PGP
- UniProt
- A6NDG6
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Phosphoglycolate phosphatase (PGP) is a conserved cytosolic hydrolase of the haloacid dehalogenase family that functions as a metabolic proofreading enzyme. It specifically dephosphorylates 2-phosphoglycolate and related damage metabolites, such as 2-phospho-L-lactate, which are generated during oxidative DNA damage repair. By clearing these metabolites, PGP prevents the inhibition of key glycolytic enzymes, including triosephosphate isomerase and phosphofructokinase, thereby maintaining metabolic flux. PGP activity is essential for embryonic development and sustained cell proliferation, as it couples the products of DNA repair to intermediary metabolism. Its critical role in cellular survival is further evidenced by its necessity for parasite viability in Plasmodium species, suggesting its importance across diverse biological systems.