Deubiquitinase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins . May therefore play an important regulatory role at the level of protein turnover by preventing degradation of proteins through the removal of conjugated ubiquitin . Specifically hydrolyzes ''Lys-63''-, ''Lys-48''-, ''Lys-29''- and ''Lys-33''-linked polyubiquitins chains . Essential component of TGF-beta/BMP signaling cascade . Specifically deubiquitinates monoubiquitinated SMAD4, opposing the activity of E3 ubiquitin-protein ligase TRIM33 . Deubiquitinates alkylation repair enzyme ALKBH3 . OTUD4 recruits USP7 and USP9X to stabilize ALKBH3, thereby promoting the repair of alkylated DNA lesions . Deubiquitinates mTORC2 complex component RICTOR at ''Lys-294'' by removing ''Lys-63''-linked polyubiquitin chains, stabilizing RICTOR and enhancing its binding to MTOR, thus promoting mTORC2 complex assembly . Regulates chromosome alignment and segregation in mitosis by regulating the localization of BIRC5/survivin to mitotic centromeres . Involved in axonal growth and neuronal cell migration . Regulates cellular clock function by enhancing the protein stability and transcriptional activity of the core circadian protein BMAL1 via its deubiquitinating activity . Acts as a regulator of peroxisome import by mediating deubiquitination of PEX5: specifically deubiquitinates PEX5 monoubiquitinated at ''Cys-11'' following its retrotranslocation into the cytosol, resetting PEX5 for a subsequent import cycle . Deubiquitinates PEG10 (By similarity).

USP9X;DFFRX; FAF; FAM; MRX99; MRXS99F

q93008

Human,Mouse,Rat

WB

WB 1:500-2000

Monoclonal

Mouse

Human recombinant protein fragment corresponding to amino acids 2246-2570 of human USP9X (NP_001034680) produced in E.coli.

Purified from mouse ascites fluids or tissue culture supernatant by affinity chromatography (protein A/G)

PBS (pH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide.

Store at +4°C short term. Store at -20°C long term. Avoid freeze / thaw cycle.