PIASy1 Antibody (C-term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| IHC-P, WB, E |
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Primary Accession | Q8N2W9 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 56504 Da |
Antigen Region | 471-499 aa |
Gene ID | 51588 |
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Other Names | E3 SUMO-protein ligase PIAS4, 632-, PIASy, Protein inhibitor of activated STAT protein 4, Protein inhibitor of activated STAT protein gamma, PIAS-gamma, PIAS4, PIASG |
Target/Specificity | This PIASy1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 471-499 amino acids from the C-terminal region of human PIASy1. |
Dilution | WB~~1:1000 IHC-P~~1:10~50 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | PIASy1 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | PIAS4 {ECO:0000303|PubMed:32832608, ECO:0000312|HGNC:HGNC:17002} |
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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 (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). |
Cellular Location | Nucleus, PML body Note=Colocalizes with SUMO1 and TCF7L2/TCF4 and LEF1 in a subset of PML (promyelocytic leukemia) nuclear bodies. |
Tissue Location | Highly expressed in testis and, at lower levels, in spleen, prostate, ovary, colon and peripheral blood leukocytes |
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Background
PIASy1 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. This protein plays a crucial role in transcriptional coregulation of various cellular pathways, including the STAT pathway, the p53 pathway, the wnt pathway and the steroid hormone signaling pathway. PIASy1 is involved in gene silencing, and promotes PARK7 sumoylation.
References
Imoto, S., et al., J. Biol. Chem. 278(36):34253-34258 (2003).
Chun, T.H., et al., Circ. Res. 92(11):1201-1208 (2003).
Subramanian, L., et al., J. Biol. Chem. 278(11):9134-9141 (2003).
Liu, B., et al., Proc. Natl. Acad. Sci. U.S.A. 98(6):3203-3207 (2001).
Liu, B., et al., Proc. Natl. Acad. Sci. U.S.A. 95(18):10626-10631 (1998).
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