Recombinant Human NOS1 protein

**Background of NOS1 Recombinant Protein**

Nitric oxide synthase 1 (NOS1), also known as neuronal NOS (nNOS), is a critical enzyme responsible for synthesizing nitric oxide (NO), a versatile signaling molecule involved in numerous physiological processes. NOS1 is predominantly expressed in neuronal tissues but is also found in skeletal muscle, epithelial cells, and other non-neuronal tissues. It plays a key role in neurotransmission, vascular regulation, immune response, and synaptic plasticity by catalyzing the conversion of L-arginine to L-citrulline and NO in a calcium/calmodulin-dependent manner. Dysregulation of NOS1 activity is linked to neurological disorders (e.g., Alzheimer’s disease, schizophrenia), cardiovascular diseases, and cancer.

Recombinant NOS1 protein is engineered through heterologous expression systems (e.g., *E. coli*, insect, or mammalian cells*) to study its structure, function, and interactions. The recombinant form typically includes affinity tags (e.g., His-tag) for purification and may retain functional domains, such as the oxygenase and reductase regions, as well as regulatory motifs like the PDZ domain for subcellular targeting. Researchers utilize NOS1 recombinant protein to investigate enzyme kinetics, post-translational modifications (e.g., phosphorylation), and its role in NO-mediated signaling pathways. It also serves as a tool for drug discovery, enabling high-throughput screening of inhibitors or activators to modulate pathological NO overproduction or deficiency. Studies leveraging recombinant NOS1 have advanced understanding of its dimerization mechanism, redox sensitivity, and interactions with scaffolding proteins (e.g., PSD-95), offering insights into therapeutic strategies for NOS1-associated diseases.