nNOS Mouse, Unlabeled, Clone: 16, BD

Nitric oxide synthase (NOS), a cell-type specific enzyme, catalyzes the synthesis of nitric oxide (NO). NO is a short-lived radical that transmits cellular signals involved in vasorelaxation, neurotransmission, and cytotoxicity. In neurons and endothelial cells, constitutive NOS (cNOS) is activated by agonists that increase intracellular Ca²⁺ levels and enhance calmodulin binding. Neuronal NOS (nNOS or bNOS) and endothelial NOS (ECNOS) have recognition sites for NADPH, FAD, FMN, and calmodulin and are regulated in a similar manner. However, both have been shown to be distinct gene products of about 155kDa and 140kDa, respectively, and the human forms show 52% amino acid identity. Neuronal NOS and induced macrophage NOS (iNOS) share 51% amino acid homology with the greatest degree of divergence in the calmodulin binding domain. Neuronal NOS, a cytosolic protein present mainly in neural tissues, has been purified and characterized from rat cerebellum. The NO synthesized by this enzyme acts as a neurotransmitter. ECNOS has been cloned from human vascular endothelium as well as from bovine aortic endothelial cells (BAEC) and has a unique N-myristylation consensus sequence that may explain its membrane localization.

Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blotting