HAUSP Antibody

3277:

Western Blotting

HAUSP Antibody detects endogenous levels of total HAUSP protein.

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Asp438 of human HAUSP. Antibodies are purified by peptide affinity chromatography.

Western blot analysis of extracts from MCF-7, NIH/3T3 and PC12 cells using HAUSP Antibody.

Ubiquitinating enzymes (UBEs) catalyze protein ubiquitination, a reversible process countered by deubiquitinating enzyme (DUB) action (1,2). Five DUB subfamilies are recognized, including the USP, UCH, OTU, MJD and JAMM enzymes. Herpesvirus-associated ubiquitin-specific protease (HAUSP, USP7) is an important deubiquitinase belonging to USP subfamily. A key HAUSP function is to bind and deubiquitinate the p53 transcription factor and an associated regulator protein Mdm2, thereby stabilizing both proteins (3,4). In addition to regulating essential components of the p53 pathway, HAUSP also modifies other ubiquitinylated proteins such as members of the FoxO family of forkhead transcription factors and the mitotic stress checkpoint protein CHFR (5,6).

1. Nijman, S.M. et al. (2005) Cell 123, 773-86.
2. Nalepa, G. et al. (2006) Nat Rev Drug Discov 5, 596-613.
3. Li, M. et al. (2002) Nature 416, 648-53.
4. Brooks, C.L. et al. (2007) Oncogene 26, 7262-6.
5. van der Horst, A. et al. (2006) Nat Cell Biol 8, 1064-73.
6. Oh, Y.M. et al. (2007) Biochem Biophys Res Commun 357, 615-9.

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For Research Use Only. Not For Use In Diagnostic Procedures.