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PIAS1 Antibody (C-Terminus)
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC-P, IF, E |
|---|---|
| Primary Accession | O75925 |
| Reactivity | Human, Mouse, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 72kDa |
| Dilution | IHC-P (5 µg/ml), WB (1-2 µg/ml), |
| Gene ID | 8554 |
|---|---|
| Other Names | E3 SUMO-protein ligase PIAS1, 6.3.2.-, DEAD/H box-binding protein 1, Gu-binding protein, GBP, Protein inhibitor of activated STAT protein 1, RNA helicase II-binding protein, PIAS1, DDXBP1 |
| Target/Specificity | Human PIAS1 |
| Reconstitution & Storage | Short term 4°C, long term aliquot and store at -20°C, avoid freeze thaw cycles. Store undiluted. |
| Precautions | PIAS1 Antibody (C-Terminus) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | PIAS1 |
|---|---|
| Synonyms | DDXBP1 |
| 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 pathway and the steroid hormone signaling pathway. In vitro, binds A/T-rich DNA. The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context. Sumoylates PML (at'Lys-65' and 'Lys-160') and PML-RAR and promotes their ubiquitin-mediated degradation. PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 which in turn promotes PML phosphorylation and degradation (By similarity). Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Plays a dynamic role in adipogenesis by promoting the SUMOylation and degradation of CEBPB (By similarity). Mediates the nuclear mobility and localization of MSX1 to the nuclear periphery, whereby MSX1 is brought into the proximity of target myoblast differentiation factor genes (By similarity). Also required for the binding of MSX1 to the core enhancer region in target gene promoter regions, independent of its sumolyation activity (By similarity). Capable of binding to the core enhancer region TAAT box in the MYOD1 gene promoter (By similarity). |
| Cellular Location | Nucleus {ECO:0000250|UniProtKB:O88907}. Nucleus speckle Nucleus, PML body {ECO:0000250|UniProtKB:O88907}. Cytoplasm, cytoskeleton. Note=Interaction with CSRP2 may induce a partial redistribution along the cytoskeleton (PubMed:11672422). Interaction with MSX1 is required for localization to the nuclear periphery (By similarity) {ECO:0000250|UniProtKB:O88907, ECO:0000269|PubMed:11672422} |
| Tissue Location | Expressed in numerous tissues with highest level in testis. |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
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 and the steroid hormone signaling pathway. In vitro, binds A/T-rich DNA. The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context. Together with PRMT1, may repress STAT1 transcriptional activity, in the late phase of interferon gamma (IFN-gamma) signaling. Sumoylates PML (at'Lys-65' and 'Lys-160') and PML-RAR and promotes their ubiquitin-mediated degradation. PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 which in turn promotes PML phosphorylation and degradation (By similarity). Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation.
References
Liu B.,et al.Proc. Natl. Acad. Sci. U.S.A. 95:10626-10631(1998).
Tan J.,et al.Mol. Endocrinol. 14:14-26(2000).
Wang P.,et al.BMC Genomics 10:518-518(2009).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Zody M.C.,et al.Nature 440:671-675(2006).
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