The UBE2R2 antibody is a research tool targeting the ubiquitin-conjugating enzyme E2 R2 (UBE2R2), a key component of the ubiquitin-proteasome system involved in protein degradation. UBE2R2. also known as CDC34B, belongs to the E2 enzyme family responsible for transferring ubiquitin to substrate proteins, often in collaboration with E3 ligases. This post-translational modification regulates diverse cellular processes, including cell cycle progression, DNA repair, and apoptosis. UBE2R2 specifically interacts with SCF (Skp1-Cul1-F-box) E3 ligase complexes, facilitating the ubiquitination of substrates like cyclin-dependent kinase inhibitors.
Antibodies against UBE2R2 are widely used in molecular biology to study its expression, localization, and function. They enable detection via techniques such as Western blotting, immunohistochemistry, and immunoprecipitation. Research has linked UBE2R2 dysregulation to several diseases, particularly cancers, where altered ubiquitination pathways contribute to tumorigenesis. For instance, UBE2R2 overexpression has been observed in certain malignancies, potentially driving uncontrolled cell proliferation.
The antibody's specificity is critical due to structural similarities between UBE2R2 and its paralog UBE2R1 (CDC34A). Some isoforms or splice variants (e.g., UBE2R2-1 and UBE2R2-2) may require validation of antibody cross-reactivity. Ongoing studies explore UBE2R2's role in therapeutic contexts, including its potential as a biomarker or drug target in precision oncology.