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anti-Mouse (Murine) PIAS1 Antikörper:
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Human Polyclonal PIAS1 Primary Antibody für IHC (p), ELISA - ABIN542816
Nishida, Yasuda: PIAS1 and PIASxalpha function as SUMO-E3 ligases toward androgen receptor and repress androgen receptor-dependent transcription. in The Journal of biological chemistry 2002
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Human Polyclonal PIAS1 Primary Antibody für IHC (p), ELISA - ABIN542815
Miyauchi, Yogosawa, Honda, Nishida, Yasuda: Sumoylation of Mdm2 by protein inhibitor of activated STAT (PIAS) and RanBP2 enzymes. in The Journal of biological chemistry 2002
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Human Polyclonal PIAS1 Primary Antibody für IHC (p), WB - ABIN388054
Tan, Hall, Hamil, Grossman, Petrusz, French: Protein inhibitors of activated STAT resemble scaffold attachment factors and function as interacting nuclear receptor coregulators. in The Journal of biological chemistry 2002
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Human Polyclonal PIAS1 Primary Antibody für ICC, IHC (p) - ABIN3044474
Scortegagna, Berthon, Settas, Giannakou, Garcia, Li, James, Liddington, Vilches-Moure, Stratakis, Ronai: The E3 ubiquitin ligase Siah1 regulates adrenal gland organization and aldosterone secretion. in JCI insight 2017
these results indicate that PIAS1 is a positive regulator of MYC.
PIAS1 overexpression exacerbated mutant Huntingtin-associated phenotypes and aberrant protein accumulation
Pias1 expression in primary myoblasts enhances the induction of cardiac muscle genes MyoD, Myogenin and Myomaker. Endothelial cell specific inactivation of Pias1 in vivo impairs yolk sac erythrogenesis, angiogenesis and recapitulates loss of myocardium muscle mass. Pias1 is an essential gene for YS erythropoiesis and vasculogenesis in vivo.
Data suggest overexpression of Pias1 in white adipose tissue (WAT) of obesity/prediabetes improves insulin resistance; knockdown of Pias1 in normal WAT leads to insulin resistance; Pias1 expression in WAT is down-regulated by c-Jun N-terminal kinase.
Between the E3 SUMO ligase PIAS1 and STAT-3.
Knockdown of PIAS1 in astrocytes impairs the accumulation of nuclear STI1 in response to irradiation. Moreover, a PIAS1 mutant lacking the STI1 binding site is unable to increase STI1 nuclear retention.
A novel role of PIAS1 in maintaining the quiescence of dormant hematopoietic stem cells and in the epigenetic repression of the myeloerythroid program.
The present study showed that PIAS1 functions as a SUMO E3 ligase of C/EBPbeta to regulate adipogenesis.
Piasy represses the synergistic activation of PITX2 with interacting co-factors and Piasy represses Pias1 activation of PITX2 transcriptional activity.
MAPK-activated protein kinase-2 limits endothelial inflammation via the PIAS1 S522 phosphorylation-mediated increase in PIAS1 transrepression and SUMO ligase activity.
Results suggest that PIAS1 may serve as a lipogenic regulator by negatively modulating liver X receptors (LXRs) in a SUMOylation-independent manner.
PIAS1 modifies covalent modification of Blimp-1 by SUMO-1 at lysine 816.
PIAS1 negatively regulates ubiquitination of Msx1 homeoprotein independent of its SUMO ligase activity.
FOXL2 interacts with PIAS1 and UBC9, and sumoylated in both human and mouse
PIAS1 restricts the differentiation of natural T(reg) cells by maintaining a repressive chromatin state of the Foxp3 promoter.
Pias1-dependent SUMOylation influences Gli protein activity
protein inhibitor of activated Stat1 (PIAS1) interacts with the tetramerization and C-terminal regulatory domains of p53 in yeast two-hybrid analyses
Protein inhibitors of activated STAT resemble scaffold attachment factors and function as interacting nuclear receptor coregulators.
PIAS1 has a role in sumoylation of focal adhesion kinase and activates its autophosphorylation
GATA4 is a SUMO-1-targeted transcription factor and together with PIAS1 is a potent regulator of cardiac gene activity
Rad18, independently of its ubiquitin ligase activity, promotes DNA polymerase eta SUMOylation by facilitating its interaction with its SUMO ligase PIAS1 and is required for DNA polymerase eta function at difficult to replicate loci.
PIAS1 as a key regulator of Epstein-Barr Virus lytic replication. PIAS1 acts as an inhibitor for transcription factors involved in lytic gene expression.
PIAS1 is a prognostic biomarker in breast cancer
PIAS1 is a determinant of poor survival and acts as a positive feedback regulator of AR signaling through enhanced AR stabilization in prostate cancer
HBs protein-induced hPIAS1 transcription requires TAL1, E47, MYOG, NFI, and MAPK signal pathways
identified the SUMO ligase PIAS1 as a constituent PML-NB antiviral protein. This finding distinguishes a SUMO ligase that may mediate signaling events important in promyelocytic leukemia nuclear body mediated intrinsic immunity.
PIAS1 enhances p300 recruitment to c-Myb-bound sites through interaction with both proteins. In addition, the E3 activity of PIAS1 enhances further its coactivation
Results show that apocrine breast cancer and prostate cancer cells share a core AR cistrome and target gene signature linked to cancer cell growth, and PIAS1 plays a similar coregulatory role for AR in both cancer cell types.
c-Myc is targeted to the proteasome for degradation in a SUMOylation-dependent manner, regulated by PIAS1, SENP7 and RNF4
Data demonstrate that PIAS1 interacts with TRF2 and mediates its sumoylation serving as a molecular switch that controls the level of TRF2 at telomeres.
the expression of SENP8, SAE1, PIAS1, PIAS2 and ZMIZ1 is deregulated in the majority of PTC tissues, likely contributing to the PTC phenotype.
Our data suggest that necdin suppresses PIAS1 both by inhibiting SUMO E3 ligase activity and by promoting ubiquitin-dependent degradation.
the presented data indicate that PIAS1 is crucial for parental and docetaxel resistant prostate cancer cell survival
Elevated PIAS1 expression was observed in breast tumor samples.
PIAS1 is the E3 ligase responsible for SUMOylation of HMGN2.
Further study indicated that PIAS1 interacted with IRF3 and inhibited the DNA binding activity of IRF3.
Levels of STAT1 andor the protein expression of its negative regulators, PIAS1 and SOCS3, may be a good predictor of hepatitis C virus response to therapy
Smad2 and PIAS1 proteins were significantly upregulated resulting in dramatically increased interactions between Smad2/4 and PIAS1 in the presence of zinc.
This gene encodes a member of the mammalian PIAS
protein inhibitor of activated STAT, 1
, DEAD/H (Asp-Glu-Ala-Asp/His) box binding protein 1
, DEAD/H box-binding protein 1
, E3 SUMO-protein ligase PIAS1
, protein inhibitor of activated STAT protein 1
, AR interacting protein
, RNA helicase II-binding protein
, gu-binding protein
, protein inhibitor of activated STAT-1
, zinc finger, MIZ-type containing 3
, SUMO E3 ligase