Anti-UBE2Q2 Antibody Picoband® Fluoro488 Conjugated

UBE2Q2 is identified as a putative ubiquitin-conjugating enzyme (E2) in a microarray screen for mitotic regulatory proteins. Its gene is mapped to 15q24.2. UBE2Q2 can covalently bind ubiquitin on the active site cysteine within the UBC domain. Inhibition of UBE2Q2 in HeLa cells causes an early mitotic arrest and increases cytotoxicity when the cells are treated with microtubule-inhibiting agents (MIAs) . Changes in cell cycle progression and viability are not observed in the absence of MIA treatment, indicating that UBE2Q2 is involved in the response to MIAs rather than performing a more general function in mitosis. Moreover, inhibition of the UBE2Q2 protein causes cells to undergo a prolonged prophase arrest, suggesting that UBE2Q2 normally functions to antagonize an early mitotic checkpoint. Finally, inhibition of UBE2Q2 also sensitizes cells to the cytotoxic effects of MIAs through caspase-mediated apoptosis that is correlated with PARP1 cleavage.

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys- 48'-linked polyubiquitination. .

1. Banerjee, S., Brooks, W. S., Crawford, D. F. Inactivation of the ubiquitin conjugating enzyme UBE2Q2 causes a prophase arrest and enhanced apoptosis in response to microtubule inhibiting agents. Oncogene 26: 6509-6517, 2007. 2. Crawford, D. F., Piwnica-Worms, H. The G2 DNA damage checkpoint delays expression of genes encoding mitotic regulators. J. Biol. Chem. 276: 37166-37177, 2001. 3. Seghatoleslam, A., Zambrano, A., Millon, R., Ganguli, G., Argentini, M., Cromer, A., Abecassis, J., Wasylyk, B. Analysis of a novel human gene, LOC92912, over-expressed in hypopharyngeal tumours. Biochem. Biophys. Res. Commun. 339: 422-429, 2006.