UBE2T polyclonal antibody

Protein ubiquitination requires the concerted action of the E1, E2, and E3 ubiquitin-conjugating enzymes. Ubiquitin is first activated through ATP-dependent formation of a thiol ester with ubiquitin-activating enzyme E1. The activated ubiquitin is then transferred to a thiol group of ubiquitin-carrier enzyme E2. The final step is the transfer of ubiquitin from E2 to an ε-amino group of the target protein lysine residue, which is mediated by ubiquitin-ligase enzyme E3.Ubiquitin conjugating-enzyme 2T (UBE2T) is an E2 family member responsible for the ATP-dependent ubiquitin tagging of target proteins for degradation. Research studies indicate that UBE2T plays an important role in the Fanconi anemia pathway and that UBE2T expression is required for normal DNA repair through this pathway. Interaction between UBE2T and FANCL appears to stimulate UBE2T auto monoubiquitination, leading to UBE2T inactivation and negative regulation of the Fanconi anemia pathway. Additional research details upregulation of UBE2T expression in breast cancer cells and certain lung carcinomas, suggesting a possible involvement in these malignancies.

Ubiquitin-conjugating enzyme E2 T; Cell proliferation-inducing gene 50 protein; E2 ubiquitin-conjugating enzyme T; Ubiquitin carrier protein T; Ubiquitin-protein ligase T; UBE2T; HSPC150; PIG50

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE) .

Western blot (WB) analysis of UBE2T polyclonal antibody at 1:500 dilution Lane1:MCF-7 whole cell lysate (40ug) Lane2:HepG2 whole cell lysate (40ug) Lane3:CT26 whole cell lysate (40ug) Lane4:C6 whole cell lysate (40ug) Lane5:H9C2 whole cell lysate (40ug)