Product Pathways - Protein Stability
USP2 Antibody #8036
|W||H Mk (Dg) (Hr)||Endogenous||68||Rabbit|
Reactivity Key: H=Human Mk=Monkey Dg=Dog Hr=Horse
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
USP2 Antibody recognizes endogenous levels of total USP2 protein. This antibody cross-reacts with all known USP2 splice variants but does not cross-react with USP21.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu387 of human USP2 protein. Antibodies are purified by protein A and peptide affinity chromatography.
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. Ubiquitin-specific-processing protease 2 (USP2) belongs to the USP (UBP/UCH type 2) subfamily and is characterized by its C19 peptidase activity, which is involved in ubiquitin recycling and in the disassembly of various forms of polymeric ubiquitin and ubiquitin-like protein complexes (3). Characteristic of the USP subfamily, USP2 possesses a highly conserved "Cys box" and "His box," which contain a conserved cysteine and histidine residue, respectively, and form part of the active site of this thiol protease. The catalytic core, which lies between the Cys box and His box, is responsible for the deubiquitinating activity of USP2 and is present within each of its splice variants (4,5).There is mounting evidence that USP2 functions as an oncoprotein through multiple mechanisms. In human prostate cancer, USP2 is highly overexpressed and drives tumor growth by binding to and stabilizing fatty acid synthase through deubiquitination (6,7). It has also been demonstrated that USP2 can bind and deubiquitinate both Mdm2 (8) and cyclin D1 (9), which leads to their stabilization and enhanced cell proliferation.
- Nijman, S.M. et al. (2005) Cell 123, 773-86.
- Nalepa, G. et al. (2006) Nat Rev Drug Discov 5, 596-613.
- Wilkinson, K.D. (1997) FASEB J 11, 1245-56.
- Gousseva, N. and Baker, R.T. (2003) Gene Expr 11, 163-79.
- Baek, S.H. et al. (1997) J Biol Chem 272, 25560-5.
- Graner, E. et al. (2004) Cancer Cell 5, 253-61.
- Priolo, C. et al. (2006) Cancer Res 66, 8625-32.
- Stevenson, L.F. et al. (2007) EMBO J 26, 976-86.
- Shan, J. et al. (2009) Mol Cell 36, 469-76.
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For Research Use Only. Not For Use In Diagnostic Procedures.