USP16 Protein, Human (Sf9)

The USP16 protein is a specific deubiquitinase that targets "Lys-120" of histone H2A (H2AK119Ub), a tag associated with epigenetic transcriptional repression. By catalytically removing this ubiquitin moiety, USP16 acts as a coactivator, promoting subsequent phosphorylation of histone H3 (H3S10ph) 'Ser-11' to achieve mitotic chromosome segregation. USP16 Protein, Human (Sf9) is the recombinant human-derived USP16 protein, expressed by Sf9 insect cells , with tag free. The total length of USP16 Protein, Human (Sf9) is 822 a.a., .

USP16 protein serves as a specific deubiquitinase, targeting 'Lys-120' of histone H2A (H2AK119Ub), a distinctive tag associated with epigenetic transcriptional repression. By catalyzing the removal of this ubiquitin moiety, USP16 acts as a coactivator, facilitating subsequent phosphorylation at 'Ser-11' of histone H3 (H3S10ph), a crucial event for chromosome segregation during mitosis. This deubiquitination process is indispensable for maintaining transcription in resting B- and T-lymphocytes, where phosphorylation by AURKB enhances USP16 activity. Furthermore, USP16 plays a regulatory role in Hox gene expression through histone H2A deubiquitination, with a preference for nucleosomal substrates. Notably, USP16 exhibits selectivity, as it does not deubiquitinate histone H2B. Beyond histones, USP16 extends its deubiquitinating activity to non-histone proteins, exemplified by its interaction with ribosomal protein RPS27A. In this context, USP16-mediated deubiquitination of monoubiquitinated RPS27A promotes the maturation of the 40S ribosomal subunit. These diverse functions highlight the multifaceted role of USP16 in the regulation of chromatin dynamics and cellular processes beyond histone modification.

Human

Sf9 insect cells

Tag Free

Q9Y5T5 (G2-L823)

10600

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.