Active, Recombinant Human UBE2G2

Background: UBE2G2 is a class I ubiquitin‑conjugating (E2) enzyme that plays a central role in ER‑associated degradation (ERAD). UBE2G2 cooperates with specific E3 ligases, notably gp78/AMFR and HRD1, to build K48‑linked polyubiquitin chains on proteins misfolded in the endoplasmic reticulum. These tagged substrates are then retrotranslocated and degraded by the 26S proteasome, maintaining ER protein quality control and limiting ER stress. UBE2G2 is largely cytosolic but functionally enriched at the ER membrane through interactions with E3s and adaptors. It is broadly expressed and partially redundant with UBE2G1, yet UBE2G2 is often the dominant ERAD E2, and its loss causes accumulation of misfolded ER clients and activation of the unfolded protein response.