抗Human PIAS4 抗体:
抗Rat (Rattus) PIAS4 抗体:
抗Mouse (Murine) PIAS4 抗体:
Human Polyclonal PIAS4 Primary Antibody for ICC, IF - ABIN269501
Tong, Shen, Wang, Kan, Wang, Li, Wang, Yang, Guo: DNA ploidy cytometry testing for cervical cancer screening in China (DNACIC Trial): a prospective randomized, controlled trial. in Clinical cancer research : an official journal of the American Association for Cancer Research 2009
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Human Polyclonal PIAS4 Primary Antibody for IF, WB - ABIN537320
Zoumpoulidou, Jones, Fernandez de Mattos, Francis, Fusi, Lee, Christian, Varshochi, Lam, Brosens: Convergence of interferon-gamma and progesterone signaling pathways in human endometrium: role of PIASy (protein inhibitor of activated signal transducer and activator of transcription-y). in Molecular endocrinology (Baltimore, Md.) 2004
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Human Polyclonal PIAS4 Primary Antibody for IHC (p), ELISA - ABIN543220
Subramanian, Benson, Iñiguez-Lluhí: A synergy control motif within the attenuator domain of CCAAT/enhancer-binding protein alpha inhibits transcriptional synergy through its PIASy-enhanced modification by SUMO-1 or SUMO-3. in The Journal of biological chemistry 2003
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Human Polyclonal PIAS4 Primary Antibody for ICC, IF - ABIN441248
Alshareeda, Negm, Green, Nolan, Tighe, Albarakati, Sultana, Madhusudan, Ellis, Rakha: SUMOylation proteins in breast cancer. in Breast cancer research and treatment 2014
Human Polyclonal PIAS4 Primary Antibody for IHC (p), IP - ABIN543219
Albor, El-Hizawi, Horn, Laederich, Frosk, Wrogemann, Kulesz-Martin et al.: The interaction of Piasy with Trim32, an E3-ubiquitin ligase mutated in limb-girdle muscular dystrophy type 2H, promotes Piasy degradation and regulates UVB-induced keratinocyte apoptosis through ... in The Journal of biological chemistry 2006
Cow (Bovine) Polyclonal PIAS4 Primary Antibody for WB - ABIN2777708
Zhang, Xu, Han, Wei, Shu: PIASy represses TRIF-induced ISRE and NF-kappaB activation but not apoptosis. in FEBS letters 2004
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PIASgamma regulates HNF-1A SUMOylation with functional implications
Study reported that RIF1 is SUMOlyated in response to DNA damage and identified PIAS4 as the primary SUMO E3 ligase required for the SUMOylation of RIF1 protein. Mammalian cells compromised of PIAS4 expression, show impaired RIF1 SUMOylation and defective for the disassembly of DNA damage responsive RIF1 foci.
Investigation of the mechanisms responsible for the alcohol action revealed that alcohol enhanced the expression of protein inhibitor of activated STAT (PIASy) and overexpression of PIASy compromised anti-hepatitis C virus ability of IFN-lambda1.
study demonstrates that Piasy may prevent exaggerated transcription of IFNI by Rbp2-mediated demethylation of H3K4me3 of IFNI, avoiding excessive immune responses
In the present study, the protein inhibitor of activated STAT Y (PIASy) was identified as a novel Isl1-interacting protein. Furthermore, PIASy and Isl1 upregulate insulin gene expression and insulin secretion in a dose-dependent manner by activating the insulin promoter.
post-translational modification of Nkx3.2 employing HDAC9-PIASy-RNF4 axis plays a crucial role in controlling chondrocyte viability and hypertrophic maturation during skeletal development in vertebrates.
new protein isoform encoded by KIAA0317, termed fibrosis-inducing E3 ligase 1 (FIEL1), which potently stimulates the TGFbeta signaling pathway through the site-specific ubiquitination of PIAS4.
these findings provide evidence for the effects of PIAsxalpha and its mechanism on osteosarcoma progression, which offers novel insight into sumoylation and the cell cycle in osteosarcoma.
PIAS4 was identified as a candidate gene for abnormal head size in 13 patients with proximal 19p13.3 submicroscopic rearrangements .
Our data reveal a novel and dynamic role for PIAS4 in the cellular-mediated restriction of herpesviruses and establish a new functional role for the PIAS family of SUMO ligases in the intrinsic antiviral immune response to DNA virus infection.
PIAS4 activity are required for the AMPKalpha1 SUMOylation and the inhibition of AMPKalpha1 activity towards mTORC1 signalling.
PIAS4 (rs735842) and VEGFA (rs699947) were the most statistically significant variants associated in hypoxia pathway analysis.
PIASgamma-dependent modification of tomosyn-1 with SUMO-2/3 presents a novel mechanism to adapt secretory strength to the dynamic synaptic environment.
SUMOylation of RXRalpha is significantly enhanced through PIAS4-mediated activity.
High reactive oxygen speciesinduces oxidation and ubiquitin-mediated degradation of PIASgamma, thereby disrupting PIASgamma-IKKgamma cross talk.
Human melanoma patient samples and cell lines maintain p53 expression but PIASy and/or Tip60 are frequently lost.
PIAS4 was overexpressed in pancreatic cancer cells compared with normal pancreas; it interacts with the tumour suppressor von Hippel-Lindau (VHL) and leads to VHL sumoylation, oligomerization and impaired function; study elucidates role of PIAS4 in regulation of pancreatic cancer cell growth
PIASgamma fully represses Nurr1 transactivation through a direct interaction, independently of its E3-ligase activity
Evidence that PIASy is the only SUMO E3 ligase that regulates lung cancer epithelial-to-mesenchymal transition (EMT) by repressing SIRT1 transcription.
Our study suggested that systemic sclerosis is associated with STAT gene rs7574865 polymorphism.
a PIAS4 homologue (zfPIAS4a) from the zebrafish model that shares many conserved structural hallmarks with the human and mammal PIAS4 proteins was successfully identified
Data suggest that PIASy exhibits a SIM (SUMO-interacting motif) in addition to the SIM identified in homologous proteins in other species; both SIMs are located near C terminus of PIASy, and both are required for full ligase activity of PIASy; hydrophobic core residues of the new SIM are essential in binding to SUMO-3. (PIASy = protein inhibitors of activated STAT y; SUMO-3 = small ubiquitin-like modifier 3)
The Xenopus PIAS genes are expressed throughout early development and have overlapping and distinct expression patterns, with, for example, strong expression of PIAS4 in the neural and neural crest derivatives.
XPIASy functions as an essential negative regulator of the XSmad2 pathway to ensure proper mesoderm induction at the appropriate time and in the appropriate region.
Data show that the Rod/Zw10 complex interacts with the first 47 residues of PIASy which are important for mitotic SUMOylation, and that depletion of Rod compromises the centromeric localization of PIASy and SUMO2/3 in mitosis.
PIAS4 mediated SIRT1 repression led to SMAD3 hyperacetylation and enhanced SMAD3 binding to fibrogenic gene promoters and PIAS4 promoted hepatic stellate cells activation in a SIRT1-dependent manner in vitro.
Findings indicate that protein inhibitor of activated STAT 4 (PIAS4) mediated SIRT1 repression in response to nutrient surplus contributes to the pathogenesis of Nonalcoholic Steatohepatitis (NASH).
PKA-induced SREBP1c sumoylation by PIASy.
the SUMO E3 ligase PIASy (also known as PIAS4) was induced by hypoxia and prevented Sp1 from binding to the SIRT1 promoter.
Piasy represses the synergistic activation of PITX2 with interacting co-factors and Piasy represses Pias1 activation of PITX2 transcriptional activity.
Protein inhibitor of activated STAT, PIASy regulates alpha-smooth muscle actin expression by interacting with E12 in mesangial cells.
PIASy negatively regulates both IFN transcription and IFN-stimulated gene expression through multiple mechanisms utilizing the function of different domains.
Studies define an important role of PIASy in hypoxia signaling through promoting HIF1alpha SUMOylation.
PIASgamma as a transcriptional co-regulator of Nurr1 and suggest that this interaction may have a physiological role in regulating the expression of Nurr1 target genes.
Piasy(-/-) mice appear phenotypically normal, activation of STAT1 is not significantly perturbed, and sumoylation patterns for SUMO-1 or SUMO-3 modification are similar in wild-type and knockout mice
Analysis of mice carrying a targeted mutation of the Piasy gene indicates that PIASy has a modest effect on cytokine and Wnt signaling, suggesting its redundancy with other members of the PIAS family.
analysis of gene regulatory interplay between TBP, PIAS1, PIAS3, PIASx, PIASy, ZFP523, and transcription factors
by controlling Piasy stability, Trim32 regulates UVB-induced keratinocyte apoptosis through induction of NFkappaB
PIASy cooperates with PIAS1 to down-regulate the specificity and magnitude of NF-kappa B/STAT1-mediated gene activation.
provide the first evidence for the existence of a close-spatially controlled-mode of regulation of FIP200 and PIASy nucleocytoplasmic functions
Data show that poly(ADP-ribose)-polymerase-1 is the DNA proximal regulator, which senses DNA strand breaks and, through poly(ADP-ribose) synthesis, assembles assembles IKKgamma, PIASy, and ATM in a dynamic manner.
Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53 pathway, the Wnt pathway and the steroid hormone signaling pathway. Involved in gene silencing. Promotes PARK7 sumoylation. In Wnt signaling, represses LEF1 and enhances TCF4 transcriptional activities through promoting their sumoylations.
E3 SUMO-protein ligase PIAS4
, protein inhibitor of activated STAT protein 4
, protein inhibitor of activated STAT protein PIASy
, protein inhibitor of activated STAT protein gamma
, zinc finger, MIZ-type containing 6
, protein inhibitor of activated STAT 4
, protein inhibitor of activated STAT, 4
, E3 SUMO-protein ligase PIAS4-like
, e3 SUMO-protein ligase PIAS4-like
, protein inhibitor of activated STAT PIASy
, protein inhibitor of activated STAT, 4b