N-Myristoyltransferase 2 (NMT2) is a key enzyme responsible for catalyzing the transfer of myristic acid, a 14-carbon saturated fatty acid, to the N-terminal glycine residues of specific substrate proteins. This post-translational modification, termed N-myristoylation, plays a critical role in regulating protein-membrane interactions, intracellular trafficking, and signal transduction. As one of two isoforms in humans (NMT1 and NMT2), NMT2 shares ~77% amino acid sequence identity with NMT1 but exhibits distinct substrate preferences and tissue-specific expression patterns.
NMT2 is ubiquitously expressed, with elevated levels observed in the brain, heart, and skeletal muscle. Its dysfunction has been implicated in various pathological processes, including cancer progression, neurodegenerative disorders, and viral pathogenesis, as many viral proteins require N-myristoylation for proper function. Antibodies targeting NMT2 are essential tools for studying its expression, localization, and interaction networks. They enable applications such as Western blotting, immunohistochemistry, and co-immunoprecipitation to explore NMT2's regulatory mechanisms and therapeutic potential.
Recent research highlights NMT2 as a biomarker and drug target, particularly in cancers where altered lipid metabolism drives tumorigenesis. Developing selective NMT2 inhibitors or modulators could offer novel strategies for disease intervention.