USP7 Overexpression Lysate

HEK293T cells in 10-cm dishes were transiently transfected with a non-lipid polymer transfection reagent specially designed and manufactured for large volume DNA transfection. Transfected cells were cultured for 48hrs before collection. The cells were lysed in modified RIPA buffer (25mM Tris-HCl pH7.6, 150mM NaCl, 1% NP-40, 1mM EDTA, 1xProteinase inhibitor cocktail mix, 1mM PMSF and 1mM Na3VO4, and then centrifuged to clarify the lysate. Protein concentration was measured by BCA protein assay kit.

HAUSP (also known as deubiquitinating enzyme 7, herpes virus associated ubiquitin specific protease, TEF1, ubiquitin carboxyl terminal hydrolase 7, ubiquitin specific protease 7, ubiquitin thiolesterase 7, and USP7) is a novel p53 interacting protein. HAUSP was identified by mass spectrometry of affinity-purified p53 associated factors by Li et al. HAUSP strongly stabilizes p53 even in the presence of excess MDM2, and also induces p53-dependent cell growth repression and apoptosis. HAUSP has an intrinsic enzymatic activity that specifically de-ubiquitinates p53 both in vivo and in vitro. Expression of a catalytically inactive point mutation of HAUSP in cells increased the levels of p53 ubiquitination and also destabilized p53. Li et al concluded that their findings revealed an important mechanism by which p53 can be stabilized by direct de-ubiquitination and also implied that HAUSP may function as a tumor suppressor in vivo through the stabilization of p53.

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Lysates are guaranteed for 6 months from date of receipt.

Array NBL1-17671

• USP7 Antibodies
• USP7 Lysate
• USP7 Protein
• USP7 Proteins and Enzyme