UBA5 (Ubiquitin-like modifier-activating enzyme 5) is a critical enzyme involved in the ubiquitin-like post-translational modification system, specifically activating ubiquitin-fold modifier 1 (Ufm1) through a cascade of ATP-dependent reactions. This process, termed ufmylation, plays essential roles in endoplasmic reticulum (ER) stress response, protein quality control, and regulation of cellular homeostasis. UBA5 is the sole E1 enzyme for Ufm1. initiating its conjugation to target proteins by forming a thioester bond with Ufm1. which is subsequently transferred to the E2 enzyme UFC1 and the E3 ligase UFL1. Dysregulation of the UBA5-Ufm1 pathway has been linked to various diseases, including cancer, neurodegenerative disorders, and diabetes. For instance, mutations in UBA5 are associated with early-onset epileptic encephalopathy and hypomyelinating leukodystrophy, highlighting its importance in neurological function.
UBA5 antibodies are indispensable tools for studying the expression, localization, and function of UBA5 in both physiological and pathological contexts. They are widely used in techniques like Western blotting, immunohistochemistry, and immunofluorescence to investigate UBA5's role in ER stress adaptation, autophagy, and tumor progression. Researchers also employ these antibodies to explore therapeutic strategies targeting the Ufm1 pathway in diseases linked to UBA5 dysfunction. High-quality UBA5 antibodies enable precise detection of endogenous UBA5 protein levels, aiding in mechanistic studies of cellular stress responses and disease pathogenesis.