3/eNOS/NOS Type III
Nitric oxide synthase (NOS), a cell-type specific enzyme, catalyzes the synthesis of nitric oxide (NO). NO is a short-lived radical that transmits signals involved in vasorelaxation, neurotransmission, and cytotoxicity. In neurons and endothelial cells, constitutive NOS (cNOS) is activated by agonists that increase intracellular Ca[2+] levels and enhance calmodulin binding. Neuronal NOS (mNOS) and endothelial NOS (eNOS) have recognition sites for NADPH, FAD, FMN, and calmodulin and both are regulated in a similar manner. The human forms exhibit 52% amino acid identity. However, they are distinct gene products of about 155 kDa (mNOS) and 140 kDA (eNOS). The eNOS gene was cloned from human vascular endothelium as well as from bovine aortic endothelial cells (BAEC). eNOS protein has a unique N-myristylation consensus sequence that may explain its membrane localization.
The specificity of this antibody conjugate for flow cytometric analysis was validated by confirming that RNA-mediated interference (RNAi) of the specific protein reduced the staining of the cells (see figure). Furthermore, the capacity of the RNAi to down-regulate the expression of the relevant protein was confirmed by western blot analysis.