USP25 Protein, Human (His)

The USP25 protein acts as a deubiquitinating enzyme and plays a key role in the hydrolysis of the ubiquitin moiety conjugated to the substrate. This function enables processing of newly synthesized ubiquitin, recycling of ubiquitin molecules, and editing of polyubiquitin chains, thus preventing proteasomal degradation of substrates. USP25 Protein, Human (His) is the recombinant human-derived USP25 protein, expressed by E. coli , with N-6*His labeled tag. The total length of USP25 Protein, Human (His) is 1054 a.a., .

Ubiquitin-specific protease 25 (USP25) is a deubiquitinating enzyme with the capacity to hydrolyze ubiquitin moieties conjugated to substrates, thereby participating in the processing of newly synthesized ubiquitin, recycling ubiquitin molecules, and editing polyubiquitin chains. USP25 plays a crucial role in preventing the proteasomal degradation of substrates by cleaving ubiquitin chains. Notably, it exhibits hydrolytic activity towards both 'Lys-48'- and 'Lys-63'-linked tetraubiquitin chains, showcasing its versatility in targeting different ubiquitin linkage types. Additionally, a muscle-specific isoform of USP25, known as USP25m, is suggested to play a role in the regulation of muscular differentiation and function, indicating its potential significance in specific cellular contexts.

Human

E. coli

N-6*His

Q9UHP3 (T2-R1055)

29761

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

<1 EU/μg, determined by LAL method.