人 ASPG 抗体对
01AB02710
Asparaginase (ASPG) is a human cytosolic enzyme that catalyzes the hydrolysis of L-asparagine into L-aspartate and ammonia, while also exhibiting distinct phospholipid-modifying activities. The protein features an N-terminal catalytic domain, requiring a critical Thr19 residue for its enzymatic functions, and a C-terminal region containing multiple ankyrin repeats that likely facilitate protein-protein interactions. Biochemical analysis reveals that ASPG operates with sigmoidal, allosteric kinetics and a relatively low affinity for L-asparagine, suggesting a regulatory role in metabolism rather than bulk catabolism. In addition to its role in asparagine and phospholipid pathways, recombinant human ASPG has demonstrated cytotoxic effects on leukemic cells through its combined asparaginase and platelet-activating factor acetylhydrolase activities, highlighting its potential significance in oncology.
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技术参数
- 靶点基因名
- ASPG
- 基因别名
- C14orf76
- 蛋白别名
- asparaginase; ASPG
- UniProt
- Q86U10
- 物种
- Human
产品详情
- 靶点名称
- ASPG
- 蛋白名称
- asparaginase
- 蛋白别名
- 60 kDa lysophospholipase; LysoLP; Lysophospholipase-transacylase) [Includes: L-asparaginase; L-asparagine amidohydrolase); 1-alkyl-2-acetylglycerophosphocholine esterase; Platelet-activating factor acetylhydrolase; PAF acetylhydrolase]
- 靶点基因名
- ASPG
- 基因别名
- C14orf76
- UniProt
- Q86U10
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Asparaginase (ASPG) is a human cytosolic enzyme that catalyzes the hydrolysis of L-asparagine into L-aspartate and ammonia, while also exhibiting distinct phospholipid-modifying activities. The protein features an N-terminal catalytic domain, requiring a critical Thr19 residue for its enzymatic functions, and a C-terminal region containing multiple ankyrin repeats that likely facilitate protein-protein interactions. Biochemical analysis reveals that ASPG operates with sigmoidal, allosteric kinetics and a relatively low affinity for L-asparagine, suggesting a regulatory role in metabolism rather than bulk catabolism. In addition to its role in asparagine and phospholipid pathways, recombinant human ASPG has demonstrated cytotoxic effects on leukemic cells through its combined asparaginase and platelet-activating factor acetylhydrolase activities, highlighting its potential significance in oncology.