SENP3 Protein, Human (GST)

The SENP3 protein is a key protease in protein sumoylation and can efficiently release SUMO2 and SUMO3 from substrates but is less active on SUMO1 conjugates. Its regulatory effects span multiple cellular processes, including dissociation of SUMO2 from MEF2D, enhancing its transcriptional activation, and dissociation from CDCA8, affecting cellular dynamics. SENP3 Protein, Human (GST) is the recombinant human-derived SENP3 protein, expressed by E. coli , with N-GST labeled tag. The total length of SENP3 Protein, Human (GST) is 274 a.a., .

SENP3 protein emerges as a pivotal protease in the intricate world of protein sumoylation, exhibiting a potent ability to release SUMO2 and SUMO3 monomers from sumoylated substrates, with weaker activity against SUMO1 conjugates. Its regulatory influence extends to various cellular processes, as SENP3 is involved in deconjugating SUMO2 from MEF2D, enhancing its transcriptional activation potential, and from CDCA8, impacting cellular dynamics. Functioning as a redox sensor, SENP3, when redistributed into the nucleoplasm, acts as an effector to boost HIF1A transcriptional activity by desumoylating EP300. It plays a vital role in rRNA processing through deconjugation of SUMO2 and SUMO3 from nucleophosmin, NPM1, while also participating in the regulation of the sumoylation status of ZNF148. Operating as a component of the Five Friends of Methylated CHTOP (5FMC) complex, SENP3 contributes to the desumoylation of ZNF148, leading to the subsequent transactivation of ZNF148 target genes. Furthermore, SENP3 deconjugates SUMO2 from KAT5 and, under oxidative stress, its degradation is impeded, resulting in its stabilization and accumulation in the nucleoplasm.

Human

E. coli

N-GST

Q9H4L4 (E301-V574)

26168

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

<1 EU/μg, determined by LAL method.