PIAS4 Antibody

Code CSB-PA030004
Size US$100
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Product Details

Uniprot No.
Target Names
PIAS4
Alternative Names
E3 SUMO protein ligase PIAS4 antibody; E3 SUMO-protein ligase PIAS4 antibody; FLJ12419 antibody; MGC35296 antibody; PAIASgamma antibody; PIAS 4 antibody; PIAS gamma antibody; PIAS-gamma antibody; Pias4 antibody; PIAS4_HUMAN antibody; PIASG antibody; PIASgamma antibody; PIASy antibody; Protein inhibitor of activated STAT 4 antibody; Protein inhibitor of activated STAT protein 4 antibody; Protein inhibitor of activated STAT protein gamma antibody; Protein inhibitor of activated STAT protein PIASy antibody; Zinc finger MIZ type containing 6 antibody; ZMIZ 6 antibody; ZMIZ6 antibody
Raised in
Rabbit
Species Reactivity
Human,Mouse
Immunogen
Synthesized peptide derived from the C-terminal region of Human PIASy.
Immunogen Species
Homo sapiens (Human)
Conjugate
Non-conjugated
Isotype
IgG
Purification Method
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Form
Liquid
Tested Applications
WB, IHC, ELISA
Recommended Dilution
Application Recommended Dilution
WB 1:500-1:2000
IHC 1:100-1:300
ELISA 1:20000
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

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Target Background

Function
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/TP53 pathway, the Wnt pathway and the steroid hormone signaling pathway. Involved in gene silencing. Mediates sumoylation of CEBPA, PARK7, HERC2, MYB, TCF4 and RNF168. In Wnt signaling, represses LEF1 and enhances TCF4 transcriptional activities through promoting their sumoylations. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation.
Gene References into Functions
  1. study demonstrates that Piasy may prevent exaggerated transcription of IFNI by Rbp2-mediated demethylation of H3K4me3 of IFNI, avoiding excessive immune responses PMID: 28970247
  2. 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. PMID: 28000708
  3. 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. PMID: 27312341
  4. 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. PMID: 27162139
  5. 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. PMID: 26708148
  6. PIAS4 was identified as a candidate gene for abnormal head size in 13 patients with proximal 19p13.3 submicroscopic rearrangements . PMID: 25853300
  7. 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. PMID: 26937035
  8. PIAS4 activity are required for the AMPKalpha1 SUMOylation and the inhibition of AMPKalpha1 activity towards mTORC1 signalling. PMID: 26616021
  9. PIAS4 (rs735842) and VEGFA (rs699947) were the most statistically significant variants associated in hypoxia pathway analysis. PMID: 25234649
  10. PIASgamma-dependent modification of tomosyn-1 with SUMO-2/3 presents a novel mechanism to adapt secretory strength to the dynamic synaptic environment. PMID: 24614299
  11. SUMOylation of RXRalpha is significantly enhanced through PIAS4-mediated activity. PMID: 26116533
  12. High reactive oxygen speciesinduces oxidation and ubiquitin-mediated degradation of PIASgamma, thereby disrupting PIASgamma-IKKgamma cross talk. PMID: 24457965
  13. 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 PMID: 24002598
  14. PIASgamma fully represses Nurr1 transactivation through a direct interaction, independently of its E3-ligase activity PMID: 23358114
  15. Evidence that PIASy is the only SUMO E3 ligase that regulates lung cancer epithelial-to-mesenchymal transition (EMT) by repressing SIRT1 transcription. PMID: 23704280
  16. Our study suggested that systemic sclerosis is associated with STAT gene rs7574865 polymorphism. PMID: 22173230
  17. PIASy binding to p53 and PIASy-activated Tip60 lead to K386 sumoylation and K120 acetylation of p53. PMID: 22751435
  18. Protein inhibitor of activated STAT, PIASy regulates alpha-smooth muscle actin expression by interacting with E12 in mesangial cells. PMID: 22829926
  19. PIAS4 and the process of SUMOylation are important modulators of Vitamin D receptor-mediated signaling PMID: 22564762
  20. The increase of NCOA3 is essential for SYT-SSX1-mediated synovial sarcoma formation. SYT-SSX1 does so by increasing the sumoylation of NCOA3 through interaction with a SUMO E3 ligase, PIASy, as well as the sumoylation of NEMO. PMID: 21454665
  21. Cav-3 is SUMOylated in a manner that is enhanced by the SUMO E3 ligase PIASy; Cav-3 SUMOylation in the mechanisms for beta(2)AR but not beta(1)AR desensitization PMID: 21362625
  22. Knockdown of PIASy by small interfering RNA leads to reduction of VHL oligomerization and increases HIF1alpha degradation PMID: 20300531
  23. Studies define an important role of PIASy in hypoxia signaling through promoting HIF1alpha SUMOylation. PMID: 20661221
  24. PIASy plays an important role in regulation of p73alpha transcriptional activity and is also a regulator of the cell cycle machinery PMID: 20471636
  25. PIASgamma directs Topoisomerase II to specific chromosome regions that require efficient removal of DNA catenations prior to anaphase. The lack of this activity activates the spindle checkpoint, protecting cells from non-disjunction. PMID: 17183683
  26. PIASy has a role in modification of C-EBPalpha by SUMO-1 or SUMO-3 PMID: 12511558
  27. PIASy suppresses GATA-2 transcriptional activity in endothelial cells. PMID: 12750312
  28. PIASy has a role in regulating TGF-beta expression along with SMAD3 PMID: 12815042
  29. PIASy may repress the androgen factor by recruiting histone deacetylases, independent of its SUMO ligase activity PMID: 14981544
  30. IFNgamma and protein inhibitor of activated STAT-y synergistically inhibited progesterone receptor-dependent transcription PMID: 15155784
  31. the inhibitory action of PIASy on BMP-regulated Smad activity was due to direct physical interactions between Smads and PIASy through its RING domain PMID: 15158472
  32. PIASy is an inhibitor of TRIF-induced ISRE and NF-kappaB activation but not apoptosis PMID: 15251447
  33. Sumoylation of Lys(35) in PIASy determines the nuclear localization of PIASy and it is necessary for PIASy-dependent sumoylation and transcriptional activation of Tcf-4. PMID: 15831457
  34. Direct interactions between the promyelocytic leukemia (PML) body protein PIASy and the Cajal body (CB) protein coilin have a role in mediating association of CBs to PML bodies. PMID: 16219678
  35. a direct role in cellular senescence and apoptosis PMID: 16793547
  36. PIASy is the first SUMO ligase for NEMO whose substrate specificity seems to be controlled by IKK interaction, subcellular targeting and oxidative stress conditions. PMID: 16906147
  37. Results report that Yin Yang 1 protein can be sumoylated both in vivo and in vitro by PIASy, a SUMO E3 ligase. PMID: 17353273
  38. PIASy controls Ets-1 function, at least in part, by inhibiting Ets-1 protein turnover via the ubiquitin-proteasome system. PMID: 17456046
  39. Our results indicate that PIASy negatively regulates E1AF-mediated transcription by both E1AF sumoylation in a dependent and independent fashion. PMID: 17585876
  40. PIASy has a role in down-regulation of MUC1 expression PMID: 17717071
  41. provide the first evidence for the existence of a close-spatially controlled-mode of regulation of FIP200 and PIASy nucleocytoplasmic functions PMID: 18285457
  42. PIASy regulates TGF-beta/Smad3-mediated signaling by stimulating sumoylation and nuclear export of Smad3. PMID: 18384750

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Subcellular Location
Nucleus, PML body. Note=Colocalizes with SUMO1 and TCF7L2/TCF4 and LEF1 in a subset of PML (promyelocytic leukemia) nuclear bodies.
Protein Families
PIAS family
Tissue Specificity
Highly expressed in testis and, at lower levels, in spleen, prostate, ovary, colon and peripheral blood leukocytes.
Database Links

HGNC: 17002

OMIM: 605989

KEGG: hsa:51588

STRING: 9606.ENSP00000262971

UniGene: Hs.105779

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