USP7 Monoclonal Antibody (USP 3D8), eBioscience™, Invitrogen™

Description

• Description: This USP 3D8 monoclonal antibody recognizes human USP7, an ubiquitin specific protease
• USP 3D8 detects a ∽128 kDa band corresponding to USP7 by Western Blot and stains USP7 in the nucleus in Immunocytochemistry/immunofluorescence
• Applications Reported: This USP 3D8 antibody has been reported for use in western blot and immunocytochemistry/immunofluorescence
• Applications Tested: This USP 3D8 antibody has been tested by western blot of human cell lysates and immunocytochemistry/immunofluorescence of human cell lines
• This may be used at less than or equal to 2 μg/mL for western blot and less than or equal to 2 μg/mL for immunocytochemistry/immunofluorescence
• USP7 or HAUSP is a ubiquitin specific protease or a deubiquitylating enzyme that cleaves ubiquitin from its substrates
• Since ubiquitylation (polyubiquitination) is most commonly associated with the stability and degradation of cellular proteins, HAUSP activity generally stabilizes its substrate proteins
• HAUSP is most popularly known as a direct antagonist of Mdm2, the E3 ubiquitin ligase for the tumor suppressor protein, p53
• Normally, p53 levels are kept low in part due to Mdm2-mediated ubiquitylation and degradation of p53
• Interestingly, in response to oncogenic insults, HAUSP can deubiquitinate p53 and protect p53 from Mdm2-mediated degradation, indicating that it may possess a tumor suppressor function for the immediate stabilization of p53 in response to stress
• Another important role of HAUSP function involves the oncogenic stabilization of p53
• Oncogenes such as Myc and E1A are thought to activate p53 through a p19 alternative reading frame (p19ARF, also called ARF)-dependent pathway, although some evidence suggests ARF is not essential in this process
• An intriguing possibility is that HAUSP provides an alternative pathway for safeguarding the cell against oncogenic insults.