iNOS (Tyr-1055)[conserved site], phospho-specific polyclonal, anti-human, mouse, rat

Background:
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, inducible NOS (iNOS, NOS-II), neuronal NOS (bNOS, NOS-I), and endothelial NOS (eNOS, ecNOS, NOS-III). The inducible form of NOS, iNOS, is Ca2+ independent and is expressed in a broad range of cell types in response to stimulation with cytokines and exposure to microbial products. Phosphorylation of iNOS may regulate its activity and stability. Src kinase-induced phosphorylation of Tyr-1055 in iNOS reduces proteasomal degradation of iNOS, leading to increased NO production. Thus, phosphorylation may be an additional control for regulating iNOS activity in response to inflammatory conditions.

Immunogen: Phospho-iNOS (Tyr-1055) synthetic peptide (coupled to carrier protein) corresponds to amino acids surrounding Tyr-1055 in human iNOS. This sequence is well conserved in rat and mouse iNOS, and has some homology to the conserved sites in eNOS (Tyr-1087) and nNOS (Tyr-1326).

Specificity: The antibody detects a 130 kDa* protein corresponding to induced NOS on SDS-PAGE immunoblots of mouse macrophages treated with LPS followed by pervanadate. The antibody also detects a 150 kDa doublet that corresponds with higher molecular weight forms of NOS, which are also observed using other anti-iNOS antibodies. In addition, the antibody detects a non-specific 120 kDa band that has not been identified.

Buffer/Storage:
Rabbit polyclonal, affinity-purified antibody 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.