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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. Additionally we are shipping ULP1 Proteins (4) and many more products for this protein.
Showing 10 out of 55 products:
Yeast Polyclonal ULP1 Primary Antibody for EIA, WB - ABIN118004
Mossessova, Lima: Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast. in Molecular cell 2000
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Human Polyclonal ULP1 Primary Antibody for EIA, IHC (p) - ABIN356754
Müller, Hoege, Pyrowolakis, Jentsch: SUMO, ubiquitin's mysterious cousin. in Nature reviews. Molecular cell biology 2001
Show all 3 references for ABIN356754
Human Polyclonal ULP1 Primary Antibody for IHC (p), WB - ABIN388047
Keane, Ettenberg, Nau, Banerjee, Cuello, Penninger, Lipkowitz: cbl-3: a new mammalian cbl family protein. in Oncogene 1999
Show all 2 references for ABIN388047
Cow (Bovine) Polyclonal ULP1 Primary Antibody for IHC, WB - ABIN2786148
Haindl, Harasim, Eick, Muller: The nucleolar SUMO-specific protease SENP3 reverses SUMO modification of nucleophosmin and is required for rRNA processing. in EMBO reports 2008
Human Polyclonal ULP1 Primary Antibody for IHC, ELISA - ABIN1533438
Yeh, Gong, Kamitani: Ubiquitin-like proteins: new wines in new bottles. in Gene 2000
The present study examined dynamic changes in SENP3 expression in the cerebral cortex and in its cellular localization.
The p53 (show TP53 Antibodies)-independent tumor suppressive functions of p19(Arf (show CDKN2A Antibodies)) may be mediated by its ability to antagonize Senp3, thereby inducing cell cycle arrest by abnormally elevating the cellular levels of SUMOylated proteins.
SENP3, which is increased in gastric cancer cells, potentiates the transcriptional activity of FOXC2 (show FOXC2 Antibodies) through de-SUMOylation, in favor of the induction of specific mesenchymal gene expression in gastric cancer metastasis.
Evidence show that mTOR (show FRAP1 Antibodies)-mediated phosphorylation of SENP3 facilitates the interaction with NPM1 (show NPM1 Antibodies), thereby promoting nucleolar targeting.
SENP3 is associated with MLL1/MLL2 (show MLL2 Antibodies) complexes and catalyzes deSUMOylation of RbBP5 (show RBBP5 Antibodies).
ROS (show ROS1 Antibodies) induced SENP3 redistribution from the nucleoli to the nucleoplasm.
In a novel adaptive pathway to extreme cell stress, dynamic changes in SENP3 stability and regulation of Drp1 (show CRMP1 Antibodies) SUMOylation are crucial determinants of cell fate.
The shift of HIF-1 (show HIF1A Antibodies) transactivation by reactive oxidative species is correlated with and dependent on the biphasic redox sensing of SENP3 that leads to the differential SENP3/p300 (show EP300 Antibodies) interaction and the consequent fluctuation in the p300 (show EP300 Antibodies) SUMOylation status.
These results suggest that SMT3IP1 is a new regulator of the p53 (show TP53 Antibodies)-Mdm2 (show MDM2 Antibodies) pathway.
Hsp90 (show HSP90 Antibodies)/SENP3 association protects SENP3 from CHIP-mediated ubiquitination and subsequent degradation, but this effect of Hsp90 (show HSP90 Antibodies) requires the presence of CHIP.
SENP3-mediated de-conjugation of SUMO2 (show SUMO2 Antibodies)/3 from promyelocytic leukemia (show PML Antibodies) is correlated with accelerated cell proliferation under mild oxidative stress.
Results demonstrate that SENP1 is the most efficient SUMO protease acting on Elk-1, and that SENP3 has little effect on Elk-1. SENP2 has an intermediate effect, but its ability to activate Elk-1 is independent from its SUMO-deconjugating activity.
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 SENP3, 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
SUMO-1-specific protease 3
, SUMO/sentrin specific protease 3
, sentrin-specific protease 3
, sentrin/SUMO-specific protease SENP3
, smt3-specific isopeptidase 1
, sentrin/SUMO-specific protease 3
, SUMO/sentrin specific peptidase 3