nNOS (C-terminal region) (clone M401), anti-human, mouse, rat

Background:
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.

Immunogen: Clone (M401) was generated from a recombinant protein that included amino acid residues within the C-terminal region of human nNOS. This human nNOS sequence has high homology with similar regions in rat and mouse nNOS.

Specificity: The antibody detects a 155 kDa* protein on SDS-PAGE immunoblots of rat and mouse brain tissue lysates, as well in the rat pituitary cell line GC.

Buffer/Storage:
Mouse monoclonal antibody purified with protein A chromatography is supplied in 100µl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.