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anti-Mouse (Murine) PIAS2 Anticorps:
anti-Human PIAS2 Anticorps:
anti-Rat (Rattus) PIAS2 Anticorps:
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Human Polyclonal PIAS2 Primary Antibody pour IHC (p), ELISA - ABIN542820
Wu, Cetinkaya, Munoz-Alonso, von der Lehr, Bahram, Beuger, Eilers, Leon, Larsson: Myc represses differentiation-induced p21CIP1 expression via Miz-1-dependent interaction with the p21 core promoter. dans Oncogene 2003
Show all 3 Pubmed References
Human Polyclonal PIAS2 Primary Antibody pour WB - ABIN6712018
Yang, Zhao, Rasul, Qin, Li, Li: PIAS1-modulated Smad2/4 complex activation is involved in zinc-induced cancer cell apoptosis. dans Cell death & disease 2013
Dog (Canine) Polyclonal PIAS2 Primary Antibody pour IHC (p), ELISA - ABIN547641
van den Akker, Ano, Shih, Wang, Pironin, Palvimo, Kotaja, Kirsh, Dejean, Ghysdael: FLI-1 functionally interacts with PIASxalpha, a member of the PIAS E3 SUMO ligase family. dans The Journal of biological chemistry 2005
Human Polyclonal PIAS2 Primary Antibody pour ELISA, WB - ABIN4345419
Saito, Novak, Piovan, Basso, Sumazin, Schneider, Crespo, Shen, Bhagat, Califano, Chadburn, Pasqualucci, Dalla-Favera: BCL6 suppression of BCL2 via Miz1 and its disruption in diffuse large B cell lymphoma. dans Proceedings of the National Academy of Sciences of the United States of America 2009
The Xenopus PIAS genes are expressed throughout early development and have overlapping and distinct expression patterns, with, for example, high levels of PIAS2 in the notochord.
A direct interaction between Pold2 and PIAS2 was confirmed by direct yeast two-hybrid.
Interaction of protein inhibitor of activated STAT 2 (PIAS2) with receptor of activated C kinase 1, RACK1.
regulates interleukin-7 receptor signaling at early commitment stages of B cell differentiation
role in activating natural resistance-associated protein 1 promoter
a transcriptional cofactor for TFII-I
Miz-1 trans-actiates Nramp1 in mice
Results show that Miz1 is required for early embryonic development during gastrulation.
Miz-1 has a role in inducing apoptosis along with MAGE-A4
study provides the first line of evidence that PIASxbeta is indispensable for osteoblast differentiation and matrix mineralization, and that this signaling molecule is located between Runx2 and osterix.
the results presented demonstrate that in heat-stressed HeLa cells, p38 MAPK pathway-dependent SUMOylation of Elk-1 and phosphorylation of PIAS2 correlate with the downregulation of transactivation by Elk-1.
PIAS1expression of PIAS1 gene was increased in patients with MS compared to healthy subjects; also, there was a significant correlation between the expression of PIAS1 and PIAS2 genes with disease severity of multiple sclerosis
results indicated that PIAS2-mediated SUMOylation constrained HCV replication
the expression of SENP8, SAE1, PIAS1, PIAS2 and ZMIZ1 is deregulated in the majority of PTC tissues, likely contributing to the PTC phenotype.
UXT is a binding protein of PIAS2, and interaction between PIAS2 and UXT may be important for the transcriptional activation of AR.
PIASxalpha is a novel SUMO E3 ligase for PTEN, and it positively regulates PTEN protein level in tumor suppression.
These findings suggest that SUMO-1 modification of MDA5 possibly via PIAS2beta may play a role in the MDA5-mediated interferon response to viral infections.
PIASx may function as a co-repressor of Stat4
Required for upregulation of a large group of genes in response to DNA damage, a function that is regulated by c-Myc, but not by 14-3-3eta and represses the expression of many genes
the repressive properties of PIASxalpha/ARIP3 require its physical interaction with FLI-1, identifying PIASxalpha as a novel corepressor of FLI-1
findings show that Epstein-Barr virus Rta interacts and colocalizes with PIASxalpha and PIASxbeta in the nucleus; these interactions seem to enhance Rta sumoylation
PIASxalpha acts as a key signal integrator that permits different responses from the same transcription factor, depending on the signaling pathway that is activated.
This gene encodes a member of the protein inhibitor of activated STAT (PIAS) family. PIAS proteins function as SUMO E3 ligases and play important roles in many cellular processes by mediating the sumoylation of target proteins. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. Isoforms of the encoded protein enhance the sumoylation of specific target proteins including the p53 tumor suppressor protein, c-Jun, and the androgen receptor. A pseudogene of this gene is located on the short arm of chromosome 4. The symbol MIZ1 has also been associated with ZBTB17 which is a different gene located on chromosome 1.
protein inhibitor of activated STAT, 2
, protein inhibitor of activated STAT X
, protein inhibitor of activated STAT2
, E3 SUMO-protein ligase PIAS2
, E3 SUMO-protein ligase PIAS2-like
, e3 SUMO-protein ligase PIAS2-like
, DAB2-interacting protein
, Msx-interacting-zinc finger
, androgen receptor-interacting protein 3
, msx-interacting zinc finger protein
, protein inhibitor of activated STAT x
, zinc finger, MIZ-type containing 4
, msx-interacting-zinc finger protein