Product Pathways - Protein Stability
USP9X Antibody #5751
|W||H M R Mk Dg||Endogenous||270||Rabbit|
Reactivity Key: H=Human M=Mouse R=Rat Mk=Monkey Dg=Dog
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
USP9X Antibody recognizes endogenous levels of total USP9X protein. This antibody may also cross-react with USP9Y.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Phe2137 of human USP9X protein. Antibodies are purified by protein A and peptide affinity chromatography.
Protein ubiquitination and deubiquitination is a reversible process catalyzed by ubiquitinating enzymes (UBEs) and deubiquitinating enzymes (DUBs) (1,2). DUBs are categorized into five subfamiles-USP, UCH, OTU, MJD, and JAMM. USP9X/hFAM is an X-linked member of the ubiquitin-specific protease (USP) subfamily of DUBs and possesses a well-conserved catalytic domain with cysteine peptidase activity, which allows for cleavage of ubiquitin and polyubiquitin conjugates. USP9X is the mammalian homolog of the Drosophila fat-facets (faf) gene, which is essential for normal eye development and viability of the early fly embryo (3,4). While USP9X expression is also critical for normal mammalian development (5-7), many of its substrates are only beginning to be elucidated. There is mounting evidence that USP9X functions in the formation of cell-cell contacts during the polarization of epithelial cells, in part through deubiquitination-dependent stabilization of molecules involved in maintaining the integrity of both adherens and tight junctions. Indeed, USP9X has been found to associate with AF-6, the β-catenin-E-cadherin complex, and EFA6 (8-11). Studies have also demonstrated that USP9X is an integral component of the TGF-β/BMP signaling cascade and regulates TGF-β responsiveness by opposing TRIM33-mediated monoubiquitination of SMAD4 (12). Recently, USP9X was shown to be overexpressed in a variety of human cancers, which was linked to enhanced cell survival and chemoresistance through its ability to deubiquitinate and stabilize the Mcl-1 oncoprotein. This evidence supports USP9X as a therapeutic target in the context of human malignancies such as follicular lymphomas and diffuse large B-cell lymphomas (13).
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