Anti-GLS2 Antibody

Phosphate-activated glutaminase, also known as Glutaminase 2 (GLS2), was initially isolated from rat liver, although it has been shown to be expressed in other tissues. Like the functionally similar, larger kidney glutaminase, GLS2 catalyzes the hydrolysis of glutamine to stoichiometric amounts of glutamate and ammonia. Expression of GLS2 is increased by p53 under both stressed and nonstressed conditions, resulting in increased levels of glutamate and alpha-ketoglutarate, which in turn results in enhanced mitochondrial respiration and ATP generation. GLS2 also regulates antioxidant defense function in cells by increasing reduced glutathione levels and decreasing ROS-levels, suggesting that GLS2 acts as a mediator of p53's role in antioxidant defense in addition to its role in energy metabolism.

GLS2 antibody was raised against an 18 amino acid synthetic peptide near the center terminus of human GLS2. The immunogen is located within amino acids 300 - 350 of GLS2.

Highly expressed in liver. Expressed in brain and pancreas. Not observed in heart, placenta, lung, skeletal muscle and kidney. Expression is significantly reduced in hepatocellular carcinomas.

Plays an important role in the regulation of glutamine catabolism. Promotes mitochondrial respiration and increases ATP generation in cells by catalyzing the synthesis of glutamate and alpha-ketoglutarate. Increases cellular anti-oxidant function via NADH and glutathione production. May play a role in preventing tumor proliferation.