Anti-USP16 Antibody Picoband® Fluoro647 Conjugated

Ubiquitin carboxyl-terminal hydrolase 16 is an enzyme that in humans is encoded by the USP16 gene. It is mapped to 21q21.3. This gene encodes a deubiquitinating enzyme that is phosphorylated at the onset of mitosis and then dephosphorylated at the metaphase/anaphase transition. It can deubiquitinate H2A, one of two major ubiquitinated proteins of chromatin, in vitro and a mutant form of the protein was shown to block cell division. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.

Ubiquitin carboxyl-terminal hydrolase 16; Deubiquitinating enzyme 16; Ubiquitin thioesterase 16; Ubiquitin-processing protease UBP-M; Ubiquitin-specific-processing protease 16; USP16; MSTP039

Present in all the tissues examined including fetal brain, lung, liver, kidney, and adult heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.

Specifically deubiquitinates 'Lys-120' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A is a prerequisite for subsequent phosphorylation at 'Ser-11' of histone H3 (H3S10ph), and is required for chromosome segregation when cells enter into mitosis. In resting B- and T-lymphocytes, phosphorylation by AURKB leads to enhance its activity, thereby maintaining transcription in resting lymphocytes. Regulates Hox gene expression via histone H2A deubiquitination. Prefers nucleosomal substrates. Does not deubiquitinate histone H2B.

1. Adorno, M., Sikandar, S., Mitra, S. S., Kuo, A., Nicolas Di Robilant, B., Haro-Acosta, V., Ouadah, Y., Quarta, M., Rodriguez, J., Qian, D., Reddy, V. M., Cheshier, S., Garner, C. C., Clarke, M. F. Usp16 contributes to somatic stem-cell defects in Down's syndrome. Nature 501: 380-384, 2013. 2. Cai, S.-Y., Babbitt, R. W., Marchesi, V. T. A mutant deubiquitinating enzyme (Ubp-M) associates with mitotic chromosomes and blocks cell division. Proc. Nat. Acad. Sci. 96: 2828-2833, 1999. 3. Joo, H.-Y., Zhai, L., Yang, C., Nie, S., Erdjument-Bromage, H., Tempst, P., Chang, C., Wang, H. Regulation of cell cycle progression and gene expression by H2A deubiquitination. Nature 449: 1068-1072, 2007.