The UBE4B (Ubiquitin-Conjugating Enzyme E4B) antibody is a crucial tool in studying the UBE4B protein, a member of the ubiquitin-proteasome system responsible for tagging cellular proteins with ubiquitin for degradation. UBE4B, also known as UFD2a, acts as an E4 ubiquitin ligase, elongating polyubiquitin chains on substrates marked by E3 ligases, thereby regulating protein turnover. It plays roles in diverse processes, including DNA repair, apoptosis, neuronal development, and cancer progression. Dysregulation of UBE4B is linked to neurodegenerative diseases (e.g., Alzheimer’s) and cancers, where it may act as an oncogene or tumor suppressor depending on context.
UBE4B antibodies are widely used in research to detect protein expression, localization, and interactions via techniques like Western blotting (WB), immunohistochemistry (IHC), and immunoprecipitation (IP). These antibodies aid in elucidating UBE4B's molecular mechanisms, such as its interaction with p53 or EGFR, and its involvement in stress response pathways. Commercial UBE4B antibodies are typically raised against specific epitopes (human or mouse-derived) and validated for specificity. Challenges include cross-reactivity with homologous proteins, emphasizing the need for rigorous validation. Overall, UBE4B antibodies are pivotal in advancing understanding of ubiquitination dynamics and therapeutic targeting in disease.