UBE2I antibody targets the ubiquitin-conjugating enzyme E2I (UBE2I), also known as UBC9. a critical component in the SUMOylation pathway. This post-translational modification involves attaching Small Ubiquitin-like Modifier (SUMO) proteins to substrate proteins, regulating diverse cellular processes such as nuclear transport, DNA repair, transcriptional regulation, and stress responses. UBE2I specifically catalyzes the transfer of SUMO from the E1 activating enzyme to target substrates, often interacting with E3 ligases for substrate specificity.
Antibodies against UBE2I are widely used in research to study its expression, localization, and function in physiological and pathological contexts. They are essential tools in techniques like Western blotting, immunoprecipitation, and immunofluorescence, helping to detect UBE2I levels in cell lines, tissues, or disease models. Dysregulation of UBE2I has been linked to cancers, neurodegenerative disorders, and immune diseases, making these antibodies valuable for exploring molecular mechanisms or therapeutic targets.
UBE2I antibodies are typically produced in hosts like rabbits or mice, with reactivity across human, mouse, and rat samples. Validation includes testing for specificity via knockout controls or siRNA knockdown. Researchers also use them to investigate SUMOylation dynamics in response to cellular stressors, DNA damage, or signaling pathway activation. Their applications extend to diagnostic research, as UBE2I overexpression in certain cancers correlates with tumor progression and poor prognosis.