Recombinant Human His6-USP19 Protein, CF

Ubiquitin specific processing protease 19 (USP19) is a 146 kDa member of the C19 peptidase family that contains two alpha crystallin domains and one MYND-type zinc finger. USP19 plays a role in the rescue of ER-associated protein degradation (ERAD) substrates such as cystic fibrosis transmembrane conductance regulator (CFTR) delta F508 and T-cell receptor-alpha (TCR alpha ) from proteasomal degradation. USP19 also interacts with the ubiquitin ligases cellular IAP 1 (cIAP1) and cIAP2. Knockdown of USP19 decreases levels of both cIAPs, whereas overexpression of USP19 results in a marked increase in cIAP levels. Although it effectively removes ubiquitin from cIAPs in vitro, USP19 may stabilize cIAP proteins in vivo mainly through deubiquitinase-independent mechanisms. Intriguingly, partial rescue of TCR alpha (but not CFTR delta F508) in the ERAD pathway is also observed using a catalytically dead USP19, suggesting that USP19 exerts a non-catalytic function for select substrates in multiple biological pathways. This recombinant protein contains amino acids a C-terminal 6-His tag.