PIAS1 Antibody [J24P15] | Primary Antibodies

Application: Reactivity: Human, Mouse, Rat, Monkey

Lane 1: RL, Lane 2: MOLT-4, Lane 3: SH-SY5Y, Lane 4: Hela

Usage Information

Dilution
WB1:1000 IF1:50 - 1:200 FCM1:50 - 1:200

Application
WB, IF, FCM

Reactivity
Human, Mouse, Rat, Monkey

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
76 kDa

Positive Control	RL cells; MOLT-4 cells; KARPAS-299 cells; NK-92 cells; SH-SY5Y cells; HeLa cells; AGS cells; SW480 cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
PIAS1 Antibody [J24P15] detects endogenous levels of total PIAS1 protein.

Clone
J24P15

Synonym(s)
PIAS1; E3 SUMO-protein ligase PIAS1; DEAD/H box-binding protein 1; E3 SUMO-protein transferase PIAS1; Gu-binding protein (GBP); Protein inhibitor of activated STAT protein 1; RNA helicase II-binding protein; DDXBP1

Background
PIAS1 (protein inhibitor of activated STAT 1), a key E3 SUMO ligase and transcriptional corepressor of the PIAS family, negatively regulates JAK/STAT signaling by interacting with STAT1 to block its DNA-binding domain and promote SUMOylation at Lys703, featuring an N-terminal SAP domain forming a unique four-helix bundle for nuclear scaffold attachment and DNA targeting, a central SP-RING zinc-binding domain (RLD) coordinating Ubc9-dependent SUMO transfer via conserved Cys/His residues, a PINIT motif for nuclear retention, and a C-terminal region with a highly acidic domain (AD), serine/threonine-rich stretches, and SUMO-interaction motif (SIM) facilitating subnuclear relocalization of targets. PIAS1 dissociates from IKKα upon Ser90 phosphorylation by inflammatory cues to bind promoters and repress interferon-inducible genes like IFITM1, cooperates with HDACs/RCOR1/KDM1 to enforce transrepression independently of SUMOylation, inhibits NF-κB p65 and Smad-mediated transcription through direct binding and cofactor recruitment, modulates p53 activity by SUMOylation to alter subnuclear foci, and drives endothelial proliferation via S100A6 induction by suppressing STAT1, while PIAS1 knockout enhances antiviral protection yet promotes atherosclerosis through dysregulated KLF2/eNOS expression. PIAS1 overexpression sustains tumor progression by blocking STAT1 tumor-suppressive effects and enhancing angiogenesis, whereas its SUMO ligase activity counters viral replication (HSV-1 restriction via PML-NBs) but fosters drug resistance via STAT3/NF-κB crosstalk, with Arg303 methylation by PRMT1 fine-tuning repressive potency post-interferon stimulation.

Background

PIAS1 (protein inhibitor of activated STAT 1), a key E3 SUMO ligase and transcriptional corepressor of the PIAS family, negatively regulates JAK/STAT signaling by interacting with STAT1 to block its DNA-binding domain and promote SUMOylation at Lys703, featuring an N-terminal SAP domain forming a unique four-helix bundle for nuclear scaffold attachment and DNA targeting, a central SP-RING zinc-binding domain (RLD) coordinating Ubc9-dependent SUMO transfer via conserved Cys/His residues, a PINIT motif for nuclear retention, and a C-terminal region with a highly acidic domain (AD), serine/threonine-rich stretches, and SUMO-interaction motif (SIM) facilitating subnuclear relocalization of targets. PIAS1 dissociates from IKKα upon Ser90 phosphorylation by inflammatory cues to bind promoters and repress interferon-inducible genes like IFITM1, cooperates with HDACs/RCOR1/KDM1 to enforce transrepression independently of SUMOylation, inhibits NF-κB p65 and Smad-mediated transcription through direct binding and cofactor recruitment, modulates p53 activity by SUMOylation to alter subnuclear foci, and drives endothelial proliferation via S100A6 induction by suppressing STAT1, while PIAS1 knockout enhances antiviral protection yet promotes atherosclerosis through dysregulated KLF2/eNOS expression. PIAS1 overexpression sustains tumor progression by blocking STAT1 tumor-suppressive effects and enhancing angiogenesis, whereas its SUMO ligase activity counters viral replication (HSV-1 restriction via PML-NBs) but fosters drug resistance via STAT3/NF-κB crosstalk, with Arg303 methylation by PRMT1 fine-tuning repressive potency post-interferon stimulation.

References
https://pubmed.ncbi.nlm.nih.gov/27559144/ https://pubmed.ncbi.nlm.nih.gov/32047143/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%