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research achievements of SENP2 are reviewed in order to understand its related functions and the underlying molecular mechanisms and provide a clue for future research on SENP2
Quantitative high-throughput screening identifies cytoprotective molecules that enhance SUMO conjugation via the inhibition of SUMO-specific protease (SENP)2.
Data show that Sentrin/SUMO specific protease (SENP2) interacts with N-myc downstream regulated gene 2 (NDRG2) and mediates the de-SUMOylation process of NDRG2.
Data demonstrate that downregulation of SENP2 is correlated with poor prognosis in bladder cancer; SENP2 inhibits TGF-beta signaling and TGF-beta-induced EMT of bladder cancer cell; and that its overexpression contributes to suppress bladder cancer cell invasion and metastasis through deSUMOylation of TGF-betaRI.
The variability of the SENP1 and SENP2 genes may play a role in breast cancer occurrence.
SENP2 inhibits MMP13 expression in BC cells through de-SUMOylation of TBL1/TBLR1, which inhibits nuclear translocation of beta-catenin.
miR-181b targets SENP2 and positively regulated NF-kappaB activity. NF-kappaB activation by DNA damage in GBM cells confers resistance to radiation-induced death.
data identify SENP2 as an important regulator of fatty acid metabolism in skeletal muscle
SENP2 regulates the transcriptional function of MEF2A via direct de-SUMOylation.
p90RSK-mediated SENP2-T368 phosphorylation is a master switch in disturbed-flow-induced signaling.
we show that WWOX required for stabilization of beta-catenin regulated by SENP2 in hepatocellular carcinoma cells
ESR1 repression by SENP2 is independent of its SUMO protease activity.
Many nucleoporins are mislocalized and, in some cases, reduced in level when SENP1 and SENP2 are codepleted.
Chromosome segregation depends on precise spatial and temporal control of sumoylation in mitosis; SENP1 and SENP2 are important mediators of this control.
The SENP1 levels are influenced by the presence of Nup153, whereas SENP2 is not sensitive to changes in Nup153 abundance.
SENP2 inhibited bladder cancer cells migration and invasion by regulating the expression of MMP13.
SENP2 plays an important role in determining the dynamics and functional outcome of MEF2A SUMOylation and transcriptional activation.
SENP2 represses glycolysis and shifts glucose metabolic strategy
SENP2 regulates hepatocellular carcinoma cell growth by modulating the stability of beta-catenin.
The SUMO-specific isopeptidase SENP2 associates dynamically with nuclear pore complexes through interactions with karyopherins and the Nup107-160 nucleoporin subcomplex.
SUMO1 (UBL1\; MIM 601912) is a small ubiquitin-like protein that can be covalently conjugated to other proteins. SENP2 is one of a group of enzymes that process newly synthesized SUMO1 into the conjugatable form and catalyze the deconjugation of SUMO1-containing species.
SUMO-1 protease 1
, SUMO-1 protease-1
, SUMO-1/Smt3-specific isopeptidase 2
, SUMO/sentrin specific protease 2
, sentrin-specific protease 2
, sentrin/SUMO-specific protease SENP2
, SMT3-specific isopeptidase 2
, SUMO1/sentrin/SMT3 specific protease 2
, Axin-associating molecule
, SUMO/sentrin specific peptidase 2