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人 PTGR2 抗体对
试剂盒

人 PTGR2 抗体对

01AB01317

Prostaglandin reductase 2 (PTGR2) is an NADPH-dependent enzyme that plays a key role in the metabolism and inactivation of prostaglandins by catalyzing the reduction of the conjugated alpha,beta-unsaturated double bond of 15-keto-prostaglandins, such as 15-keto-PGE2, 15-keto-PGE1, and their alpha isomers, with highest activity toward these substrates. PTGR2 belongs to the medium-chain dehydrogenase/reductase superfamily and features a unique NADPH binding-induced conformational change in its LID motif and a polyproline type II helix, both critical for its catalytic function. Structural studies have shown that mutations in key residues like Tyr64 and Tyr259 significantly affect catalysis and substrate affinity, and that the enzyme's active site exhibits notable plasticity, especially upon inhibitor binding. Functionally, PTGR2-mediated prostaglandin inactivation is important for regulating processes such as adipocyte differentiation and insulin sensitivity, and its inhibition has been linked to potential therapeutic effects in metabolic diseases. Disease associations include evidence that silencing PTGR2 increases reactive oxygen species, suppresses pancreatic cell proliferation, and promotes cell death, suggesting a role in cancer cell survival and redox balance.

Human
规格起售价
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技术参数

靶点基因名
PTGR2
基因别名
ZADH1
蛋白别名
prostaglandin reductase 2; PTGR2
UniProt
Q8N8N7
物种
Human

产品详情

靶点名称
PTGR2
蛋白名称
prostaglandin reductase 2
蛋白别名
Prostaglandin reductase 2; PRG-2; 15-oxoprostaglandin 13-reductase; Zinc-binding alcohol dehydrogenase domain-containing protein 1
靶点基因名
PTGR2
基因别名
ZADH1
UniProt
Q8N8N7
来源物种
Homo sapiens (Human)
物种反应性
Human

背景介绍

Prostaglandin reductase 2 (PTGR2) is an NADPH-dependent enzyme that plays a key role in the metabolism and inactivation of prostaglandins by catalyzing the reduction of the conjugated alpha,beta-unsaturated double bond of 15-keto-prostaglandins, such as 15-keto-PGE2, 15-keto-PGE1, and their alpha isomers, with highest activity toward these substrates. PTGR2 belongs to the medium-chain dehydrogenase/reductase superfamily and features a unique NADPH binding-induced conformational change in its LID motif and a polyproline type II helix, both critical for its catalytic function. Structural studies have shown that mutations in key residues like Tyr64 and Tyr259 significantly affect catalysis and substrate affinity, and that the enzyme's active site exhibits notable plasticity, especially upon inhibitor binding. Functionally, PTGR2-mediated prostaglandin inactivation is important for regulating processes such as adipocyte differentiation and insulin sensitivity, and its inhibition has been linked to potential therapeutic effects in metabolic diseases. Disease associations include evidence that silencing PTGR2 increases reactive oxygen species, suppresses pancreatic cell proliferation, and promotes cell death, suggesting a role in cancer cell survival and redox balance.