USP7 Protein, Human, Recombinant (aa 208-560) is expressed in Baculovirus insect cells. The predicted molecular weight is 41 kDa and the accession number is Q93009-1.

Human

Baculovirus Insect Cells

TEF1,HAUSP,ubiquitin specific peptidase 7 (herpes virus-associated)

The amino acid sequence (Lys 208-Glu 560) of Human USP7 (NP_003461.2) expressed and purified, with two additional aa (Gly & Pro) at the N-terminus.

> 80 % as determined by SDS-PAGE

A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information.

It is recommended to store recombinant proteins at -20°C to -80°C for future use. Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.

Ubiquitin carboxyl-terminal hydrolase 7, also known as Ubiquitin thioesterase 7, Herpesvirus-associated ubiquitin-specific protease, Ubiquitin-specific-processing protease 7, USP7 and HAUSP, is a widely expressed protein that belongs to the peptidase C19 family. USP7 is a member of the family of deubiquitinating enzymes. It is involved in the regulation of stress response pathways, epigenetic silencing and the progress of infections by DNA viruses. USP7 is a protein with a cysteine peptidase core, N- and C-terminal domains required for protein-protein interactions. USP7 contributes to epigenetic silencing of homeotic genes by Polycomb (Pc). USP7 cleaves ubiquitin fusion protein substrates. It deubiquitinates TP53/p53 and MDM2 and strongly stabilizes TP53 even in the presence of excess MDM2. USP7 also induces TP53-dependent cell growth repression and apoptosis. USP7 has key roles in the p53 pathway whereby it stabilizes both p53 and MDM2. Herpes simplex virus type 1 (HSV-1) regulatory protein ICP stimulates lytic infection and the reactivation of quiescent viral genomes. ICP interacts very strongly with USP7. USP7-mediated stabilization of ICP is dominant over ICP-induced degradation of USP7 during productive HSV-1 infection. The biological significance of the ICP-USP7 interaction may be most pronounced in natural infection situations, in which limited amounts of ICP are expressed.