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anti-Mouse (Murine) PIAS3 Antikörper:
anti-Human PIAS3 Antikörper:
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Human Polyclonal PIAS3 Primary Antibody für IHC (p), WB - ABIN1882116
Nojiri, Joh, Miura, Sakata, Nomura, Nakao, Sobue, Ohara, Asai, Ito: ATBF1 enhances the suppression of STAT3 signaling by interaction with PIAS3. in Biochemical and biophysical research communications 2004
Show all 8 Pubmed References
Human Polyclonal PIAS3 Primary Antibody für IHC (p), WB - ABIN1882115
Long, Wang, Matsuura, He, Liu: Activation of Smad transcriptional activity by protein inhibitor of activated STAT3 (PIAS3). in Proceedings of the National Academy of Sciences of the United States of America 2004
Show all 7 Pubmed References
Human Polyclonal PIAS3 Primary Antibody für IHC - ABIN6712019
Yang, Zhao, Rasul, Qin, Li, Li: PIAS1-modulated Smad2/4 complex activation is involved in zinc-induced cancer cell apoptosis. in Cell death & disease 2013
Suppressed Th17 levels correlated with upregulated expression of negative regulatory genes, PIAS3, SHP2, and SOCS3 in CD4 T cells during acute SIV infection.
Results show that PIAS3 levels are reduced in a mouse model of atherosclerotic lesions and that its expression decreases in conjunction with increases in interleukin-6 expression and disease severity. These findings provide evidence that results indicate that PIAS3 is a critical repressor of atherosclerosis progression.
Data indicate that PIAS3 (protein inhibitor of activated STAT3) interaction modulates EKLF (erythroid Kruppel-like factor) activity in a promoter-dependent and SUMO-independent manner.
PIAS3 suppresses acute graft-versus-host disease by modulating effector T and B cell subsets through inhibition of STAT3 activation.
These data indicate that tachypacing decreased ATBF1, leading to enhanced STAT3 DNA-binding activity due to the reduced formation of a binary complex of ATBF1 and PIAS3.
MRL/lpr mice have significantly increased expressions of STAT3 mRNA and protein and decreased expression of mRNA PIAS3 in the kidneys compared with BALB/C mice.
L97A, R99N and R99Q mutations of the PINIT domain (PIAS3(85-272) ) were found to abrogate binding to STAT3, suggesting that these residues were part of a potential binding surface.
Our results indicate that Pias3-dependent SUMOylation of photoreceptor-specific transcription factors is a common mechanism that controls both rod and cone photoreceptor subtype specification, regulating distinct molecular targets in the two cell types
there is an interaction between Zimp7 and PIAS proteins with higher preference for PIAS3, in androgen receptor-mediated transcription
results indicate a potential role of PIAS3 as transcriptional modulator of TIF2-mediated signalling
role in inducing SUMO-1 modification and transcriptional repression of IRF-1
identified a novel conserved domain of 180 residues in PIAS proteins and showed that its 'PINIT' motif as well as other conserved motifs (in the SAP box and in the RING domain) are independently involved in nuclear retention of PIAS3L
Zip domain is the region of MITF that is involved in the direct interaction between MITF and PIAS3.
The interplay between Mitf, Pias3, and Stat3 was studied in mast cell and melanocytes.
Taken together, these data suggest that PIAS3 may play an inhibitory role in adipogenesis by modulating insulin-activated transcriptional activation events.
analysis of gene regulatory interplay between TBP, PIAS1, PIAS3, PIASx, PIASy, ZFP523, and transcription factors
The overexpression of PIAS3 attenuates osteoclast formation and down-regulates the expression of NFATc1 and osteoclast-associated receptor (OSCAR), which are important modulators in osteoclastogenesis.
PIAS3 is a new regulator of ATF1 that regulates the ARE-mediated transcription of the ferritin H gene
PIAS3 negatively regulates RANKL-mediated osteoclastogenesis directly in osteoclast precursors and indirectly via osteoblasts.
Our data thus identify Pias3-mediated SUMOylation of photoreceptor-specific transcription factors as a key mechanism of rod specification.
Concomitant gain of pSTAT3 Tyr705 and loss of PIAS3 appear critical for initiation and development of high-grade serous carcinoma.
Study reports that SMAD6 is overexpressed in nuclei of glioma cells, which correlates with poor patient survival and regulates STAT3 activity via negatively regulating PIAS3. Mechanically, SMAD6 interacts directly with PIAS3, and this interaction is mediated through the Mad homology 2 domain of SMAD6 and the Ring domain of PIAS3.
PAI-1 interacted with PIAS3 to regulate Stat3-dependent gene expression and miR-34a was transcriptionally suppressed by Stat3 to form a positive regulatory loop through Stat3 signaling in non-small cell lung cancer cells.
Levels of PIAS3 are significantly lower, in contrast with phosphorylation of STAT3, in women with endometriosis compared to women without endometriosis.
TRIM8 activates STAT3 by suppressing the expression of PIAS3, an inhibitor of STAT3, most likely through E3-mediated ubiquitination and proteasomal degradation.
Low PIAS3 expression is associated with breast cancer organoid invasiveness.
SHP2, SOCS3 and PIAS3 levels are reduced in medulloblastomas in vivo and in vitro, of which PIAS3 downregulation is more reversely correlated with STAT3 activation. In resveratrol-suppressed medulloblastoma cells with STAT3 downregulation and decreased incidence of STAT3 nuclear translocation, PIAS3 is upregulated, the SHP2 level remains unchanged and SOCS3 is downregulated.
The results revealed that although the expression levels of SOCS1, SOCS3 and, in particular, pSHP2, tend to decrease in the four types of astrocytomas, PIAS3 downregulation is more negatively correlated with STAT3 activation in the stepwise progress of astrocytomas and would indicate an unfavorable outcome.
3-Formylchromone inhibits proliferation and induces apoptosis of multiple myeloma cells by abrogating STAT3 signaling through the induction of PIAS3.
PIAS3 may serve as a biomarker for predicting hormone therapy stratification, although it is limited to those breast cancer patients receiving hormone therapy.
Taken together, these results suggest that PIAS3 functions as a positive regulator of HIF-1alpha-mediated transcription by increasing its protein stability.
PIAS3 suppression may be protective against joint destruction in rheumatoid arthritis by regulating synoviocyte migration, invasion, and activation.
PIAS3 primes ATR for checkpoint activation.
PIAS3 expression in squamous cell lung cancer is low and predicts overall survival
Adenovirus E4-ORF3 targets PIAS3 and together with E1B-55K remodels SUMO2/SUMO3 Interactions in the nucleus and at virus genome replication domains.
Statistically significant positive correlation has been found between STAT5B and COX-2, and significant negative correlation between STAT5B and PIAS3.
Low PIAS3 expression in malignant mesothelioma is associated with increased STAT3 activation and poor patient survival.
this newly identified p53PIAS3 interaction through the 1-52 amino acid region of p53, reduces p53MDM2 complex formation, which not only increases the half-life of p53, but also its transactivation of target genes.
PIAS3 may be a potential biomarker target for early cancer detection and therapeutic of human colorectal cancer.
PIAS3 activates the intrinsic apoptotic pathway in non-small cell lung cancer cells independent of p53 status.
This gene encodes a member of the PIAS
protein inhibitor of activated STAT, 3
, E3 SUMO-protein ligase PIAS3-like
, e3 SUMO-protein ligase PIAS3-like
, E3 SUMO-protein ligase PIAS3
, protein inhibitor of activated STAT protein 3
, zinc finger, MIZ-type containing 5
, potassium channel regulatory protein KChAP
, potassium channel-associated protein