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The reversible posttranslational modification of proteins by the addition of small ubiquitin-like SUMO proteins (see SUMO1\; MIM 601912) is required for numerous biologic processes.
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Mild oxidative stress stabilized the SENP5 protein in the oral squamous cell carcinoma cells, and only the combination of SENP5 silencing and H2O2 application led to mitochondria fragmentation and a significant increase in cell apoptosis.
Low expression of SENP5 is associated with good prognosis among breast cancer patients.
Knockdown of SENP5 resulted in increased levels of SUMO-1 (zeige SUMO1 Proteine) and SUMO-2 (zeige SUMO2 Proteine)/3, inhibition of cell proliferation, defects in nuclear morphology, and appearance of binucleate cells, revealing an essential role for SENP5 in mitosis and/or cytokinesis.
altered subcellular localization of SENP5 in oral squamous cell carcinoma (OSCC) cells and the correlation between SENP5 expression and the differentiation of OSCC.
Nucleolar protein (zeige MCRS1 Proteine) B23/nucleophosmin (zeige NPM1 Proteine) regulates the vertebrate SUMO pathway through SENP3 (zeige ULP1 Proteine) and SENP5 proteases.
The reversible posttranslational modification of proteins by the addition of small ubiquitin-like SUMO proteins (see SUMO1\; MIM 601912) is required for numerous biologic processes. SUMO-specific proteases, such as SENP5, are responsible for the initial processing of SUMO precursors to generate a C-terminal diglycine motif required for the conjugation reaction. They also have isopeptidase activity for the removal of SUMO from high molecular mass SUMO conjugates (Di Bacco et al., 2006
SUMO1/sentrin specific protease 5
, sentrin-specific protease 5
, sentrin/SUMO-specific protease SENP5
, SUMO/sentrin specific protease 5
, Sumo1/sentrin/SMT3 specific peptidase 5
, SUMO/Smt3-specific isopeptidase 3
, SUMO1/sentrin specific peptidase 5
, sentrin/SUMO-specific protease 5
, sentrin-specific protease 5-like