Recombinant Human NOS2 protein

Nitric oxide synthase 2 (NOS2), also known as inducible nitric oxide synthase (iNOS), is a critical enzyme responsible for catalyzing the production of nitric oxide (NO) from L-arginine. Unlike its constitutive isoforms (NOS1 and NOS3), NOS2 is typically absent under normal physiological conditions but is rapidly induced in response to inflammatory stimuli, such as cytokines (e.g., TNF-α, IFN-γ) or microbial pathogens. This induction occurs primarily in immune cells (e.g., macrophages), epithelial cells, and hepatocytes. NO generated by NOS2 plays dual roles: it serves as a key antimicrobial agent in host defense by disrupting pathogen metabolism, while excessive or prolonged production contributes to tissue damage in chronic inflammatory diseases, including sepsis, asthma, and neurodegenerative disorders.

Recombinant NOS2 protein is engineered through molecular cloning techniques, often expressed in heterologous systems like *E. coli*, insect cells, or mammalian cell lines. Its production enables detailed biochemical characterization, including studies on enzyme kinetics, post-translational modifications, and interactions with inhibitors or cofactors (e.g., tetrahydrobiopterin, calmodulin). Researchers utilize recombinant NOS2 to investigate regulatory mechanisms of NO signaling, screen potential therapeutic compounds targeting inflammatory pathways, and model disease-associated mutations. Challenges in producing functional recombinant NOS2 include maintaining solubility, stability, and proper dimerization, as the enzyme requires multiple cofactors for activity. Advances in protein engineering and purification strategies have improved yields and activity retention, facilitating its application in drug discovery and mechanistic studies. Current research focuses on modulating NOS2 activity to balance its protective and detrimental effects, offering potential therapies for inflammation-related conditions.