ATE1 (Arginyltransferase 1) is an evolutionarily conserved enzyme that catalyzes post-translational arginylation, a process critical for protein degradation and cellular regulation. This enzyme transfers arginine residues to N-terminal aspartate or glutamate of proteins, marking them for ubiquitination and proteasomal degradation via the N-end rule pathway. ATE1-mediated arginylation plays roles in diverse biological processes, including cardiovascular development, stress response, and cell cycle regulation.
ATE1 antibodies are essential tools for studying its expression, localization, and functional mechanisms. These antibodies are typically developed in model organisms (e.g., rabbit, mouse) using immunogenic peptides derived from conserved regions of ATE1. They enable detection of ATE1 in techniques like Western blotting, immunohistochemistry, and immunofluorescence. Research using ATE1 antibodies has revealed its involvement in pathological conditions, such as cardiomyopathy, neurodegeneration, and cancer metastasis. For example, ATE1 deficiency or dysregulation has been linked to impaired protein quality control and abnormal nitric oxide signaling.
The development of isoform-specific ATE1 antibodies (humans have four splice variants) has further advanced understanding of its tissue-specific functions. These reagents remain pivotal in exploring arginylation’s broader roles in cellular homeostasis and disease, highlighting ATE1 as a potential therapeutic target.