There is intense interest in metabolic enzymes and associated pathways as drug targets for a range of human pathologies including cancer, and cardiovascular, neurodegenerative, and inflammatory diseases. R&D Systems continues to expand our portfolio of active enzymes and we are pleased to now offer Recombinant Human Arginase 2 and Lipoprotein Lipase (LPL).
Arginases are critical to the urea cycle, and influence downstream nitric oxide and polyamine levels. Arginase 2, specifically, is a mitochondrial enzyme expressed in kidney, prostate, and immune cells where it is regulated by inflammatory cytokines. It is implicated in nitric oxide-dependent inflammatory responses in the lung and in neuronal disorders such as Huntington's disease. It also promotes tumorigenesis through immune suppression, metabolism, cell proliferation, and vascularization.
LPL is a rate-limiting enzyme responsible for the hydrolysis of triglycerides. It is highly controlled by regulatory factors such as apolipoproteins, angiopoietins, and hormones. It can be produced by macrophages and this expression is a critical event in the pathogenesis of atherosclerosis. Variants of LPL have been associated with altered risk of several diseases including coronary heart disease, cerebrovascular accidents, and Alzheimer's disease. LPL expression is a prognostic marker in B cell chronic lymphocytic leukemia and has been linked to solid tumor cell proliferation.
A
| ARG2 Specific Activity (pmol/min/µg) | |
| R&D Systems | 406,000 |
| Competitor | 291,000 |
B
C
Active Arginase 2 and Lipoprotein Lipase A. Recombinant Human Arginase 2 (Catalog # 9767-AR) exibits higher specific activity than the competition as measured by the production of urea during the hydrolysis of arginine. B. Recombinant Human Lipoprotein Lipase (Catalog # 9888-LL) activity is measured by its ability to hydrolyze 4-Nitrophenyl butyrate. C. Recombinant Mouse ANGPTL3 (Catalog # 9899-AN) dose dependently inhibits Recombinant Human LPL activity.