Protein myristoylation involves the attachment of myristic acid to the N-terminal glycine of proteins, catalyzed by N-myristoyl transferase. Myristoylation facilitates association of modified proteins with cellular membranes, essential for correct localization and for mediating protein-membrane and protein-protein interactions, key for signaling proteins such as kinases and GTPases. Myristoylation can increase protein stability, enhance folding, and enable conformational changes “myristoyl switches”, allowing proteins to reversibly expose or sequester the myristoyl group in response to environmental cues. Dysregulation of myristoylation is implicated in various diseases, including cancer, neurodegenerative disorders, and infections. AkrivisBio’s Protein Myristoylation Assay is an easy way to assess this process using FACS or fluorescence microscopy.
