Protein ubiquitination controls many intracellular processes, including cell cycle progression, transcriptional activation, and signal transduction. This dynamic process, involving ubiquitin conjugating enzymes and deubiquitinating enzymes, adds and removes ubiquitin. Deubiquitinating enzymes are cysteine proteases that specifically cleave ubiquitin from ubiquitin-conjugated protein substrates. This gene encodes a deubiquitinating enzyme which lies in a gene cluster on chromosome Xp11.23

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Flow cytometric analysis of Ubiquitin specific peptidase 11 expression in HeLa cells using Ubiquitin specific peptidase 11 antibody . Green, isotype control; red, Ubiquitin specific peptidase 11.

Immunocytochemical staining of HeLa cells with Ubiquitin specific peptidase 11 antibody . Nuclei were stained blue with DAPI; Ubiquitin specific peptidase 11 was stained magenta with Alexa Fluor® 647. Images were taken using Leica stellaris 5. Protein abundance based on laser Intensity and smart gain: High. Scale bar, 20 μm.

Western blotting analysis using ubiquitin specific peptidase 11 antibody . Total cell lysates (30 μg) from various cell lines were loaded and separated by SDS-PAGE. The blot was incubated with ubiquitin specific peptidase 11 antibody and HRP-conjugated goat anti-rabbit secondary antibody respectively. Image was developed using NaQ™ ECL Substrate Kit .

Western blotting analysis using ubiquitin specific peptidase 11 antibody . Ubiquitin specific peptidase 11 expression in wild type (WT) and ubiquitin specific peptidase 11 (USP11) knockdown (KD) HSHC cells with 20 μg of total cell lysates. Hsp90 α serves as a loading control. The blot was incubated with ubiquitin specific peptidase 11 antibody and HRP-conjugated goat anti-rabbit secondary antibody respectively. Image was developed using NaQ™ ECL Substrate Kit .

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