UBE2D2 Polyclonal Antibody, PerCP-Cy5.5 Conjugated

Ubiquitin is an abundant, highly conserved protein found in all eukaryotic cells either free or covalently attached to cellular proteins. The primary function of ubiquitin in mammalian systems is to clear abnormal, foreign, and improperly folded proteins by targeting them for proteosome degradation. UBE2D proteins, including UBE2D1 (ubiquitin-conjugating enzyme E2D1 or UBC5A), UBE2D2 (ubiquitin-conjugating enzyme E2D2 or UBC5B) and UBE2D3 (ubiquitin-conjugating enzyme E2D3 or UBC5C), are E2 ubiquitin-conjugating enzymes that catalyze the ubiquitination of I˚ Bå in a phosphorylation and SCFB-TRCP-dependent manner. Specifically, E1 first transfers a ubiquitin residue to the E2 component (a UBE2D protein), and the UBE2D protein then associates with an E3 ubiquitin-protein ligase, which immediately transfers that residue to a protein that is targeted for degradation.

PUBC 1; PUBC1; UB2D2_HUMAN; UBC 4; UBC 4/5; UBC4; UBC4/5; UBC4/5 homolog yeast; UBCH 5B; UBCH5B; UBE2D2; Ubiquitin carrier protein; Ubiquitin carrier protein D2; Ubiquitin conjugating enzyme E2 17 kDa 2; Ubiquitin conjugating enzyme E2 D2; Ubiquitin conjugating enzyme E2D 2 homologous to yeast UBC4/5; Ubiquitin conjugating enzyme E2D 2 UBC4/5 homolog yeast; Ubiquitin conjugating enzyme E2D 2; Ubiquitin protein ligase D2; Ubiquitin-conjugating enzyme E2 D2; Ubiquitin-conjugating enzyme E217KB 2; Ubiquitin-conjugating enzyme E2-17 kDa 2; Ubiquitin-protein ligase D2; E217KB2.