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AB58416

Anti-E3 SUMO-protein ligase PIAS4/PIASy antibody

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(7 Publications)

Rabbit Polyclonal E3 SUMO-protein ligase PIAS4/PIASy antibody. Suitable for IHC-P, WB and reacts with Human samples. Cited in 7 publications. Immunogen corresponding to Synthetic Peptide within Human PIAS4.

View Alternative Names

PIASG, PIAS4, E3 SUMO-protein ligase PIAS4, PIASy, Protein inhibitor of activated STAT protein 4, Protein inhibitor of activated STAT protein gamma, PIAS-gamma

2 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-E3 SUMO-protein ligase PIAS4/PIASy antibody (AB58416)
  • IHC-P

Unknown

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-E3 SUMO-protein ligase PIAS4/PIASy antibody (AB58416)

IHC image of ab58416 staining in human testis formalin fixed paraffin embedded tissue section, performed on a Leica BondTM system using the standard protocol F. The section was pre-treated using heat mediated antigen retrieval with sodium citrate buffer (pH6, epitope retrieval solution 1) for 20 mins. The section was then incubated with ab58416, 5µg/ml, for 15 mins at room temperature and detected using an HRP conjugated compact polymer system. DAB was used as the chromogen. The section was then counterstained with haematoxylin and mounted with DPX.

For other IHC staining systems (automated and non-automated) customers should optimize variable parameters such as antigen retrieval conditions, primary antibody concentration and antibody incubation times.

Western blot - Anti-E3 SUMO-protein ligase PIAS4/PIASy antibody (AB58416)
  • WB

Unknown

Western blot - Anti-E3 SUMO-protein ligase PIAS4/PIASy antibody (AB58416)

All lanes:

Western blot - Anti-E3 SUMO-protein ligase PIAS4/PIASy antibody (ab58416) at 1/500 dilution

Lane 1:

Jurkat cell extract without immunizing peptide

Lane 2:

Jurkat cell extract with immunizing peptide

Predicted band size: 56 kDa

Observed band size: 57 kDa

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Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

IHC-P, WB

applications

Immunogen

Synthetic Peptide within Human PIAS4. The exact immunogen used to generate this antibody is proprietary information.

Q8N2W9

Specificity

Detects endogenous levels of PAIAS gamma total protein.

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Purification notes
Affinity purified from rabbit antiserum by affinity chromatography using epitope specific immunogen.
Storage buffer
pH: 7.4 Preservative: 0.02% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine), 0.87% Sodium chloride
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Storage information
Stable for 12 months at -20°C

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The E3 SUMO-protein ligase PIAS4 also known as PIASy functions as an E3-type small ubiquitin-like modifier (SUMO) ligase. This protein plays a role in SUMOylation a post-translational modification process where it catalyzes the transfer of SUMO from E2 conjugating enzyme to target substrates. PIAS4 has a mass of approximately 57 kDa and is expressed in various tissues including the brain heart and skeletal muscle. It shows localization in the nucleus reflecting its role in regulating nuclear processes.
Biological function summary

This protein modulates transcription by interacting with and modifying transcription factors through SUMOylation affecting their stability and activity. PIAS4 participates in multiprotein complexes which can influence gene expression and cellular responses to stress. Its role in DNA repair processes is significant as it SUMOylates proteins involved in homologous recombination and DNA damage response pathways aiding in maintaining genomic integrity.

Pathways

PIAS4 plays a role in the regulation of DNA damage repair and the STAT signaling pathway. It cooperates with proteins like BRCA1 and RAD51 in DNA repair ensuring the correct repair of double-strand breaks. In the STAT signaling pathway PIAS4 influences STAT transcription factors impacting various cellular activities including growth and apoptosis. This modulation links PIAS4 to cellular responses relevant to growth and stress.

PIAS4 has connections to cancer and neurodegenerative diseases. Mutations or altered expression of PIAS4 can disrupt DNA repair processes leading to an increased susceptibility to cancer due to accumulated genomic instability. PIAS4 also interacts with proteins like p53 in pathways associated with cancer development. Additionally its involvement in stress response mechanisms could link it to neurodegenerative diseases possibly through affecting neuronal cell survival and function.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

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 (PubMed : 12511558, PubMed : 12631292, PubMed : 12727872, PubMed : 15831457, PubMed : 15976810, PubMed : 22508508, PubMed : 32832608). Mediates sumoylation of ALKBH5, AXIN1, CEBPA, KLF8, GATA2, PARK7, HERC2, MYB, TCF4 and RNF168 (PubMed : 12223491, PubMed : 12511558, PubMed : 12631292, PubMed : 12727872, PubMed : 12750312, PubMed : 15831457, PubMed : 15976810, PubMed : 16617055, PubMed : 22508508, PubMed : 34048572). 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 (PubMed : 11388671). Involved in gene silencing (PubMed : 11248056). In Wnt signaling, represses LEF1 and enhances TCF4 transcriptional activities through promoting their sumoylations (PubMed : 12727872, PubMed : 15831457). Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation (PubMed : 21965678). Binds to AT-rich DNA sequences, known as matrix or scaffold attachment regions (MARs/SARs) (By similarity). Catalyzes conjugation of SUMO2 to KAT5 in response to DNA damage, facilitating repair of DNA double-strand breaks (DSBs) via homologous recombination (HR) (PubMed : 32832608). Mediates sumoylation of PARP1 in response to PARP1 trapping to chromatin (PubMed : 35013556). Mediates sumoylation of KLF8, repressiing KLF8 transcriptional activity and cell cycle progression into G(1) phase (PubMed : 16617055). Sumoylates ALKBH5 downstream of MAPK8/JNK1 and MAPK9/JNK2 in response to reactive oxygen species (ROS), inhibiting ALKBH5 RNA demethylase activity (PubMed : 34048572).
See full target information PIAS4

Publications (7)

Recent publications for all applications. Explore the full list and refine your search

Molecular biology of the cell 34:br6 PubMed36989032

2023

p97/VCP drives turnover of SUMOylated centromeric CCAN proteins and CENP-A.

Applications

Unspecified application

Species

Unspecified reactive species

Sebastiaan J W van den Berg,Samuel East,Sreyoshi Mitra,Lars E T Jansen

Nucleic acids research 50:3922-3943 PubMed35253893

2022

ZMYM2 restricts 53BP1 at DNA double-strand breaks to favor BRCA1 loading and homologous recombination.

Applications

Unspecified application

Species

Unspecified reactive species

Doohyung Lee,Katja Apelt,Seong-Ok Lee,Hsin-Ru Chan,Martijn S Luijsterburg,Justin W C Leung,Kyle M Miller

Science advances 6:eaba7822 PubMed32832608

2020

TIP60 K430 SUMOylation attenuates its interaction with DNA-PKcs in S-phase cells: Facilitating homologous recombination and emerging target for cancer therapy.

Applications

Unspecified application

Species

Unspecified reactive species

Shan-Shan Gao,Hua Guan,Shuang Yan,Sai Hu,Man Song,Zong-Pei Guo,Da-Fei Xie,Yike Liu,Xiaodan Liu,Shimeng Zhang,Ping-Kun Zhou

Nucleus (Austin, Tex.) 9:87-94 PubMed29095668

2017

SUMO modification system facilitates the exchange of histone variant H2A.Z-2 at DNA damage sites.

Applications

Unspecified application

Species

Unspecified reactive species

Atsuhiko Fukuto,Masae Ikura,Tsuyoshi Ikura,Jiying Sun,Yasunori Horikoshi,Hiroki Shima,Kazuhiko Igarashi,Masayuki Kusakabe,Masahiko Harata,Naoki Horikoshi,Hitoshi Kurumizaka,Yoshiaki Kiuchi,Satoshi Tashiro

Nature communications 6:8979 PubMed26616021

2015

SUMOylation of AMPKα1 by PIAS4 specifically regulates mTORC1 signalling.

Applications

Unspecified application

Species

Unspecified reactive species

Yan Yan,Saara Ollila,Iris P L Wong,Tea Vallenius,Jorma J Palvimo,Kari Vaahtomeri,Tomi P Mäkelä

The Journal of cell biology 193:867-84 PubMed21624955

2011

PKCζ mediates disturbed flow-induced endothelial apoptosis via p53 SUMOylation.

Applications

Unspecified application

Species

Unspecified reactive species

Kyung-Sun Heo,Hakjoo Lee,Patrizia Nigro,Tamlyn Thomas,Nhat-Tu Le,Eugene Chang,Carolyn McClain,Cynthia A Reinhart-King,Michael R King,Bradford C Berk,Keigi Fujiwara,Chang-Hoon Woo,Jun-ichi Abe

The Journal of biological chemistry 286:14830-41 PubMed21362625

2011

Caveolin-3 undergoes SUMOylation by the SUMO E3 ligase PIASy: sumoylation affects G-protein-coupled receptor desensitization.

Applications

WB

Species

Human

Stephen R Fuhs,Paul A Insel
View all publications

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