UBE2G2 (D8Z4G) Rabbit Monoclonal Antibody #63182

Ubiquitin (Ub) is a conserved polypeptide that is covalently linked to many cellular proteins through the process of ubiquitination, which targets proteins for degradation by the 26S proteasome. Three enzymatic components are involved in the protein ubiquitination cascade. Ubiquitin is first activated by forming a thioester complex with an E1 ubiquitin-activating enzyme. Activated ubiquitin is subsequently transferred to an E2 ubiquitin-carrier protein, and then from the E2 to an E3 ubiquitin ligase for final delivery to the ε-amino group of the target protein lysine residue (1-3).
The ubiquitin-conjugating enzyme E2 G2 (UBE2G2, UBC7) is a ubiquitously expressed E2 enzyme and critical component of the endoplasmic reticulum-associated degradation pathway (ERAD) (4). Research studies demonstrate that UBE2G2 forms homodimers and preassembles K48-linked poly-Ub chains at its active site (5-8). The association of Ub-charged UBE2G2 molecules with the ER-resident E3 ligase AMFR (gp78) is required for Ub chain transfer and efficient removal of misfolded or aggregated proteins through the ERAD pathway (9,10).