人 PRKAG3 抗体对
01AB02528
Protein kinase AMP-activated non-catalytic subunit gamma 3 (PRKAG3) is the muscle-specific regulatory subunit of the AMP-activated protein kinase (AMPK) heterotrimer. As a critical energy sensor, it monitors cellular ATP, AMP, and ADP ratios to maintain metabolic homeostasis. PRKAG3 contains CBS domains that bind these adenine nucleotides, allowing it to allosterically modulate the catalytic activity of the AMPK alpha subunit. In skeletal muscle, particularly fast-twitch fibers, PRKAG3 activation promotes catabolic pathways such as glucose uptake and fatty acid oxidation while inhibiting anabolic processes. Clinically, gain-of-function mutations in PRKAG3, such as the R225W variant, are well-documented to significantly increase muscle glycogen content and enhance post-exercise glucose metabolism. These associations link the protein to quantitative trait loci (QTL) for skeletal muscle glycogen metabolism and metabolic disorders such as Fanconi-Bickel Syndrome, highlighting its central role in systemic energy regulation and exercise physiology.
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技术参数
- 靶点基因名
- PRKAG3
- 基因别名
- AMPKG3
- 蛋白别名
- protein kinase AMP-activated non-catalytic subunit gamma 3; PRKAG3
- UniProt
- Q9UGI9
- 物种
- Human
产品详情
- 靶点名称
- PRKAG3
- 蛋白名称
- protein kinase AMP-activated non-catalytic subunit gamma 3
- 蛋白别名
- 5'-AMP-activated protein kinase subunit gamma-3; AMPK gamma3; AMPK subunit gamma-3
- 靶点基因名
- PRKAG3
- 基因别名
- AMPKG3
- UniProt
- Q9UGI9
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Protein kinase AMP-activated non-catalytic subunit gamma 3 (PRKAG3) is the muscle-specific regulatory subunit of the AMP-activated protein kinase (AMPK) heterotrimer. As a critical energy sensor, it monitors cellular ATP, AMP, and ADP ratios to maintain metabolic homeostasis. PRKAG3 contains CBS domains that bind these adenine nucleotides, allowing it to allosterically modulate the catalytic activity of the AMPK alpha subunit. In skeletal muscle, particularly fast-twitch fibers, PRKAG3 activation promotes catabolic pathways such as glucose uptake and fatty acid oxidation while inhibiting anabolic processes. Clinically, gain-of-function mutations in PRKAG3, such as the R225W variant, are well-documented to significantly increase muscle glycogen content and enhance post-exercise glucose metabolism. These associations link the protein to quantitative trait loci (QTL) for skeletal muscle glycogen metabolism and metabolic disorders such as Fanconi-Bickel Syndrome, highlighting its central role in systemic energy regulation and exercise physiology.