UBE2E1 is a class III E2 ubiquitin conjugating enzyme that belongs to the UBE2E family of E2s, comprising UBE2E1/UBCH6, UBE2E2/UBCH8, and UBE2E3/UBCH9. UBE2E family members share a highly conserved UBC domain but are distinguished from one another by their unique N-terminal extensions. UbE2E1 contains a 50-residue unstructured N-terminal extension rich in serine and lysine residues, which has been shown to interact with USP7 and is essential for USP7-mediated UbE2E1 stabilization. In addition to its ubiquitin conjugating activity, UBE2E1 can also act as an ISG15 conjugating enzyme in vitro, although this activity has not been shown to occur in vivo. UBE2E1 can be covalently modified with either ISG15 or ubiquitin, both of which interfere with the ubiquitin conjugating activity of UBE2E1. UBE2E1 has also been reported to monoubiquitinate histone H2A at K119 in concert with the PRC1 E3 ligase complex. Full-length UBE2E1 is reported to be a dimer, with dimerization mediated by interaction of residues 21-27 from one molecule with the core domain of another molecule, as well as by contacts between a1 of the two interacting molecules. (PMID: 28073915, PMID: 30282802, PMID: 23871895)

-25 ~ -15℃保存，收到货之后有效期1年，避免反复冻融。