INOS (C-terminal region) Antibody

Nitric oxide (NO) has a broad range of biological activities and is implicated in signaling pathways in phylogenetically diverse species. Nitric oxide synthases (NOS), the enzymes responsible for synthesis of NO, are homodimers whose monomers are themselves two fused enzymes: a cytochrome reductase and a cytochrome that requires three cosubstrates (L-arginine, NADPH, and oxygen) and five cofactors or prosthetic groups (FAD, FMN, calmodulin, tetrahydrobiopterin, and heme) . Several distinct NOS isoforms are produced from three distinct genes. These include two constitutive Ca2+/CaM-dependent forms of NOS: nNOS (also designated bNOS, NOS-I), whose activity was first identified in neurons and eNOS (also designated ecNOS, NOS-III) first identified in endothelial cells. The inducible form of NOS, iNOS (also designated NOS-II), is Ca2+ independent and is expressed in a broad range of cell types. This form of NOS is induced after stimulation with cytokines and exposure to microbial products.

Amino acid residues within the C-terminal region of human iNOS. The human iNOS sequence used has high homology with similar regions in rat and mouse iNOS.

The antibody detects a 130 kDa* protein on SDS-PAGE immunoblots of mouse macrophages (RAW264.7) treated with IFNγ and LPS, or J774A.1 cells treated with LPS only.