Recombinant Human Arginase 2/ARG2 Protein, CF

Arginase-2, a binuclear manganese-dependent metalloenzyme, is an approximately 36 kDa protein that forms a trimeric active molecule that catalyses the conversion of L-arginine into L-ornithine and urea (1). There are two isoforms of human arginase that share 58% sequence identity. Arginases are critical to the urea cycle and also influence downstream nitric oxide and polyamine levels (2) and hence are implicated to play a role in a number of diseases. While Arginase 1 is cytosolic and expressed predominantly in the liver, Arginase 2 is a mitochondrial enzyme expressed in several non-hepatic tissues including kidney, prostate and immune cells where it is regulated by inflammatory cytokines (2,3). Arginase 2 is implicated in regulation of a nitric oxide-dependent inflammatory response in lung and bronchial epithelial disease (4,5).  It has been implicated in neuronal disease such as Huntington's disease due to nitric oxide signaling and suppressed enzymatic activity (6) and to play a role in atherosclerosis and hypertension through signaling pathways independent of its enzymatic activity (7,8). Arginase 2 promotes tumorigenesis through immune suppression, metabolism, cell proliferation and vascularization (9-11). Arginase-2 was noted as an attractive tumor therapeutic target (10) given that genetic deletion in mice does not lead to significant abnormalities (12).