Also known as: His₆-USP7_FL (HAUSP)

USP7 (Herpes-Associated Ubiquitin Specific Protease) is a nuclear protein that was initially identified as a novel p53-interacting protein. The enzyme deubiquitinates p53 thus stabilizing the levels of this key tumor suppressor, and inducing p53-dependent cell growth repression and apoptosis. USP7 also indirectly affects p53 stability by deubiquitinating HDMX, a regulator of HDM2. Full-length USP7 (1102 amino acids) contains an N-terminal p53 binding domain and 2 highly conserved USP active site domains. The C-terminal domain interacts with HSV-1 protein ICP0. This enzyme is able to cleave model substrates including linear Ub fusions, poly- ubiquitinated EBNA1 and poly-ubiquitinated p53. This recombinant protein has an N-terminal his tag & residues 213-548 representing the catalytic domain (CD) of USP7. Accession # NP_003461.