This antibody reacts with the ~160 kDa nNOS protein and does not exhibit any cross-reactivity with the related eNOS or iNOS proteins. During development reactivity was confirmed with a ~160 kD band on western blots of rat and mouse brain tissue lysates (20 µg). For use in immunohistochemistry with paraffin embedded tissues some background staining was evident.
Nitric oxide (NO) is an inorganic, gaseous free radical that carries a variety of messages between cells. As a potent bioregulatory molecule, NO plays important roles in the regulation of a variety of normal developmental and physiological processes. Vasorelaxation, neurotransmission, and cytotoxicity can all be potentiated through cellular response to NO. NO is generated by nitric oxide synthase (NOS) in a reaction that converts L-arginine and oxygen into L-citrulline and nitric oxide. Three distinct mammalian genes have been cloned and identified, which encode NOS isoforms: neuronal or brain (nNOS or bNOS), macrophage or inducible (iNOS), and endothelial (eNOS). The NOS isoforms can be subdivided into two general categories, constitutive or inducible, based on differences in their regulation and activities. All NOS isoforms contain calmodulin, nicotinamide adenine dinucleotide phosphate ( NADPH), flavin adenine dinucleotide (FAD), and flavin mononucleotide (FMN) binding domains. bNOS and eNOS share approximately 50% sequence homology and their enzymatic activity depends on binding to the calcium/calmodulin complex. The constitutive isoforms include eNOS and nNOS. These isoforms are always present but remain inactive until an increase in intracellular calcium results in enhanced calcium/calmodulin binding and subsequent activation. Increases in intracellular calcium lead to the production of low levels of NO over a short time. In contrast, the inducible NOS isoform, iNOS, is not normally expressed, but is induced (though alterations in gene expression, mRNA stability, or protein synthesis) in response to certain cytokines. The nomenclature of the NOS family members suggests restricted isoform expression patterns; however, this is misleading. For example, the 160 kDa neuronal-type NO synthase (nNOS) has been detected in a variety of cell types including neurons, epithelial cells, mesangial cells, and skeletal muscle cells, as well as in peripheral nerve cells, macula densa, and pancreatic islet cells. Alternate splicing specifically regulates nNOS in striated muscle. The translated protein, nNOS mu, is 34 amino acid residues larger than nNOS from brain.
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Protein Aliases: BNOS; brain; Constitutive NOS; IHPS1; N-NOS; NC-NOS; Neuronal NOS; nitric oxidase synthase; nitric oxide synthase 1 (neuronal); Nitric oxide synthase, brain; nNOS; NOS; NOS type I; NOS1; Peptidyl-cysteine S-nitrosylase NOS1
Gene Aliases: 2310005C01Rik; Bnos; N-NOS; NC-NOS; nNOS; NO; NOS; Nos-1; NOS-I; Nos1