The UBE2J2 antibody is a tool used to detect and study UBE2J2. a member of the ubiquitin-conjugating enzyme (E2) family. UBE2J2 plays a critical role in the ubiquitin-proteasome system (UPS), a major pathway for protein degradation and post-translational modification. Specifically, UBE2J2 is involved in endoplasmic reticulum-associated degradation (ERAD), where it collaborates with E3 ubiquitin ligases to tag misfolded or damaged proteins with ubiquitin molecules, marking them for proteasomal destruction. This enzyme is anchored to the endoplasmic reticulum (ER) membrane and participates in maintaining cellular proteostasis, stress responses, and quality control mechanisms.
Antibodies targeting UBE2J2 are essential for investigating its expression, localization, and functional interactions. They are widely used in techniques like Western blotting, immunofluorescence, and immunoprecipitation to study UBE2J2’s role in physiological and pathological contexts. Research has linked UBE2J2 dysregulation to diseases such as cancer, neurodegenerative disorders (e.g., Alzheimer’s), and metabolic syndromes, highlighting its potential as a therapeutic target. For example, reduced UBE2J2 activity may impair ERAD, leading to toxic protein aggregation, while its overexpression might influence tumor progression or drug resistance.
These antibodies also aid in exploring UBE2J2’s structural features, regulatory mechanisms (e.g., phosphorylation), and interactions with substrates or partners in the UPS. Their specificity and reliability are critical for advancing insights into cellular protein regulation and disease pathways.