USP21 Protein, Human (GST)

USP21 protein is a multifunctional deubiquitinase that plays a key role in the regulation of epigenetic transcriptional repression by deubiquitinating histone H2A. As a coactivator, it relieves the inhibition of dimethylation and trimethylation of histone H3 at "Lys-4", thereby regulating transcription initiation. USP21 Protein, Human (GST) is the recombinant human-derived USP21 protein, expressed by E. coli , with N-GST labeled tag. The total length of USP21 Protein, Human (GST) is 564 a.a., .

USP21, a multifunctional deubiquitinase, plays a pivotal role in the epigenetic regulation of transcriptional repression by specifically deubiquitinating histone H2A, acting as a coactivator and relieving the repression of di- and trimethylation of histone H3 at 'Lys-4', thus modulating transcriptional initiation. This regulatory function extends to gene expression modulation through histone H2A deubiquitination. Additionally, USP21 stabilizes BAZ2A/TIP5 through deubiquitination, demonstrating its involvement in the maintenance of protein stability. Furthermore, USP21 exhibits the capability to remove NEDD8 from NEDD8 conjugates without affecting Sentrin-1 conjugates. Notably, it acts as a negative regulator of the ribosome quality control (RQC) by mediating the deubiquitination of 40S ribosomal proteins RPS10/eS10 and RPS20/uS10, thereby counteracting ZNF598-mediated 40S ubiquitination and influencing the intricate dynamics of cellular processes.

Human

E. coli

N-GST

Q9UK80 (P2-L565)

27005

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

<1 EU/μg, determined by LAL method.