The UBE2O antibody is a research tool designed to detect and study UBE2O (Ubiquitin-Conjugating Enzyme E2 O), a unique enzyme in the ubiquitin-proteasome system. UBE2O functions as a hybrid E2-E3 ligase, combining ubiquitin-conjugating (E2) and substrate recognition (E3-like) activities in a single polypeptide. This 130 kDa protein contains an N-terminal substrate-binding domain and a C-terminal catalytic domain, enabling it to directly ubiquitinate specific targets without requiring separate E3 partners.
UBE2O plays roles in erythroid differentiation, cellular stress responses, and protein quality control by mediating non-canonical ubiquitination (including monoubiquitination and multi-monoubiquitination) of substrates like BAP1. MLL, and SMAD1/5. Its abnormal expression has been linked to hematological disorders, solid tumors, and metabolic diseases. The antibody is crucial for investigating UBE2O's localization, expression patterns, and molecular interactions in various pathological contexts.
Common applications include Western blotting (detecting endogenous UBE2O at ~130 kDa), immunoprecipitation studies, and immunohistochemical analysis. Researchers use this reagent to explore UBE2O's emerging roles in cellular processes like ribophagy, epigenetic regulation, and cancer progression. Recent studies highlight its potential as a therapeutic target, particularly in malignancies showing chromosome 17q25 amplification where UBE2O is overexpressed. Validation typically involves knockout cell lines to confirm specificity.