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Suppressed Th17 levels correlated with upregulated expression of negative regulatory genes, PIAS3, SHP2, and SOCS3 in CD4 T cells during acute SIV infection.
Data indicate that PIAS3 (protein inhibitor of activated STAT3) interaction modulates EKLF (erythroid Kruppel-like factor (show KLF1 Proteins)) 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 (show STAT3 Proteins) activation.
These data indicate that tachypacing decreased ATBF1, leading to enhanced STAT3 (show STAT3 Proteins) DNA-binding activity due to the reduced formation of a binary complex of ATBF1 and PIAS3.
MRL/lpr (show FAS Proteins) mice have significantly increased expressions of STAT3 (show STAT3 Proteins) 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 (show STAT3 Proteins), 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 (show PIAS1 Proteins) proteins with higher preference for PIAS3, in androgen receptor (show AR Proteins)-mediated transcription
results indicate a potential role of PIAS3 as transcriptional modulator of TIF2 (show NCOA2 Proteins)-mediated signalling
role in inducing SUMO-1 (show SUMO1 Proteins) modification and transcriptional repression of IRF-1 (show IRF1 Proteins)
identified a novel conserved domain of 180 residues in PIAS (show PIAS1 Proteins) proteins and showed that its 'PINIT' motif as well as other conserved motifs (in the SAP (show APCS Proteins) box and in the RING domain) are independently involved in nuclear retention of PIAS3L
PAI-1 (show SERPINE1 Proteins) interacted with PIAS3 to regulate Stat3 (show STAT3 Proteins)-dependent gene expression and miR (show MLXIP Proteins)-34a was transcriptionally suppressed by Stat3 (show STAT3 Proteins) to form a positive regulatory loop through Stat3 (show STAT3 Proteins) signaling in non-small cell lung cancer cells.
Levels of PIAS3 are significantly lower, in contrast with phosphorylation of STAT3 (show STAT3 Proteins), in women with endometriosis compared to women without endometriosis.
TRIM8 (show TRIM8 Proteins) activates STAT3 (show STAT3 Proteins) by suppressing the expression of PIAS3, an inhibitor of STAT3 (show STAT3 Proteins), most likely through E3-mediated ubiquitination and proteasomal degradation.
Low PIAS3 expression is associated with breast cancer organoid invasiveness.
SHP2 (show PTPN11 Proteins), SOCS3 (show SOCS3 Proteins) and PIAS3 levels are reduced in medulloblastomas in vivo and in vitro, of which PIAS3 downregulation is more reversely correlated with STAT3 (show STAT3 Proteins) activation. In resveratrol-suppressed medulloblastoma cells with STAT3 (show STAT3 Proteins) downregulation and decreased incidence of STAT3 (show STAT3 Proteins) nuclear translocation, PIAS3 is upregulated, the SHP2 (show PTPN11 Proteins) level remains unchanged and SOCS3 (show SOCS3 Proteins) is downregulated.
The results revealed that although the expression levels of SOCS1 (show SOCS1 Proteins), SOCS3 (show SOCS3 Proteins) and, in particular, pSHP2, tend to decrease in the four types of astrocytomas, PIAS3 downregulation is more negatively correlated with STAT3 (show STAT3 Proteins) 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 (show STAT3 Proteins) 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 (show HIF1A Proteins)-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.
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