Human Arginase 1/ARG1 PE-conjugated Antibody

Arginase 1 (ARG1) is a 35‑40 kDa member of the arginase family of enzymes. It is expressed in multiple cell types, including erythrocytes, hepatocytes, neutrophils, smooth muscle and macrophages. ARG1 demonstrates two distinct functions: in the hepatocyte cytoplasm, it catalyzes the conversion of arginine to ornithine and urea, while in multiple cells, it degrades arginine, thus indirectly downregulating NO synthase (NOS) activity by depriving this enzyme of its substrate. Human ARG1 is 322 amino acids (aa) in length. Its enzyme region comprises aa 9‑309 and contains two Mn atoms. ARG1 is moderately active as a monomer, but highly active as a 105 kDa homotrimer. Trimerization is promoted by nitrosylation of Cys303, creating a regulatory feedback loop with NOS. There are two isoform variants, one that shows an eight aa insertion after Gln43, and another that shows a deletion of aa 204‑289. Full-length human ARG1 shares 87% aa identity with mouse and rat ARG1.