COPS5 Protein, Human

The COPS5 protein is a possible protease subunit of the COP9 signalosome complex (CSN) and regulates the ubiquitin conjugation pathway by demethylating the cullin subunit of the SCF-type E3 ligase complex. This activity reduces Ubl ligase activity, affecting complexes such as SCF, CSA, or DDB2. COPS5 Protein, Human is the recombinant human-derived COPS5 protein, expressed by E. coli , with tag free. The total length of COPS5 Protein, Human is 256 a.a., .

The COPS5 protein serves as the probable protease subunit within the COP9 signalosome complex (CSN), a vital regulator involved in diverse cellular and developmental processes. Operating as a crucial component of the CSN complex, COPS5 plays a central role in the regulation of the ubiquitin conjugation pathway by facilitating the deneddylation of the cullin subunits within SCF-type E3 ligase complexes. This deneddylation activity results in the reduction of Ubl ligase activity, impacting complexes such as SCF, CSA, or DDB2. Moreover, the CSN complex, in association with CK2 and PKD kinases, is implicated in the phosphorylation of various substrates, including p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1, and IRF8. COPS5 likely functions as the catalytic center mediating the cleavage of Nedd8 from cullins within the complex, thereby influencing the regulatory landscape of protein degradation. Its direct interaction with numerous proteins regulated by the CSN complex underscores its key role in mediating cellular processes and highlights its involvement in the proteasomal degradation of BRSK2.

Human

E. coli

Tag Free

Q92905 (A2-T257)

10987

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

<1 EU/μg, determined by LAL method.