UBE2C monoclonal 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 2C (UBE2C) is one of several ubiquitin conjugating enzymes participating in the E3 anaphase-promoting complex (APC/C) . UBE2C is involved in the control of multiple stages of the cell cycle including inactivation of the mitotic spindle assembly checkpoint. UBE2C facilitates ubiquitin-dependent proteasomal degradation by initiating K11-linked ubiquitin chains on APC/C substrates. Research studies show that UBE2C expression is low in normal tissues, but its expression is dramatically upregulated in tumors derived from tissues such as lung, breast, and prostate. Overexpression of UBE2C in many types of solid tumors has been attributed to genomic amplification of the UBE2C locus and research studies have suggested that inhibition of UBE2C activity may have therapeutic potential.