NONO Antibody
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Description
NONO Antibody Overview
The NONO antibody (Catalog: 11058-1-AP) is a rabbit-derived polyclonal antibody developed by Proteintech. It recognizes the NONO protein across multiple species, including humans, mice, rats, and zebrafish . Key characteristics include:
Antiviral Mechanisms
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Flavivirus Replication: NONO binds to the replication complexes of flaviviruses (e.g., Zika, Japanese encephalitis) via interactions with viral NS3 protein and 3' UTR RNA. It facilitates positive-strand RNA synthesis, critical for viral proliferation .
Tumorigenesis and Cancer
NONO acts as an oncogenic scaffold in cancers such as triple-negative breast cancer (TNBC) and bladder cancer:
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Gene Regulation: Stabilizes oncogenic mRNAs (e.g., MYC, CCND1) and enhances transcription factors like STAT3 and nuclear EGFR .
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Therapeutic Target: High NONO expression correlates with poor prognosis and chemoresistance in TNBC .
Innate Immunity
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PRRSV Inhibition: In swine, NONO interacts with porcine reproductive and respiratory syndrome virus (PRRSV) N protein and IRF3, forming a complex that activates IFN-β signaling and suppresses viral replication .
Validation in Key Studies
Experimental Optimization
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Cross-Reactivity: Detects zebrafish and bovine NONO homologs despite being primarily validated in humans/mice .
Implications and Future Directions
The NONO antibody has enabled discoveries in virology and oncology, highlighting NONO’s dual role as a host defense modulator and oncogenic driver. Ongoing research explores its potential as a biomarker for antiviral therapies or cancer prognostics . Challenges include resolving its context-dependent roles—pro-viral in flaviviruses versus antiviral in PRRSV—and developing isoform-specific detection tools .
Product Specs
Buffer
PBS with 0.1% Sodium Azide, 50% Glycerol, pH 7.3. Store at -20°C. Avoid freeze / thaw cycles.
Lead Time
Typically, we can ship the products within 1-3 business days after receiving your order. Delivery time may vary depending on the purchasing method or location. Please consult your local distributors for specific delivery details.
Synonyms
52 kDa subunit antibody; 54 kDa nuclear RNA and DNA binding protein antibody; 54 kDa nuclear RNA- and DNA-binding protein antibody; 55 kDa nuclear protein antibody; DNA binding p52/p100 complex 52 kDa subunit antibody; DNA-binding p52/p100 complex antibody; NMT 55 antibody; NMT55 antibody; Non Pou domain containing octamer (ATGCAAAT) binding protein antibody; Non POU domain containing octamer binding antibody; Non POU domain containing octamer binding protein antibody; Non-POU domain-containing octamer-binding protein antibody; Nono antibody; NonO protein antibody; NONO_HUMAN antibody; NRB 54 antibody; NRB antibody; NRB54 antibody; Nuclear RNA binding protein 54kD antibody; P54 antibody; p54(nrb) antibody; p54nrb antibody; PPP1R114 antibody; Protein phosphatase 1 regulatory subunit 114 antibody
Target Names
NONO
Uniprot No.
Target Background
Function
NONO, a DNA- and RNA binding protein, plays a crucial role in various nuclear processes. It binds to the canonical octamer sequence in double-stranded DNA, as well as to single-stranded DNA and RNA at a site independent of the duplex site. NONO is involved in pre-mRNA splicing, likely as a heterodimer with SFPQ. It interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. In collaboration with PSPC1, NONO is required for the formation of nuclear paraspeckles. The SFPQ-NONO heteromer, associated with MATR3, might play a role in nuclear retention of defective RNAs. The SFPQ-NONO heteromer could be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1. Additionally, the SFPQ-NONO heteromer may participate in DNA non-homologous end joining (NHEJ), essential for double-strand break repair and V(D)J recombination. It might also stabilize paired DNA ends. In vitro studies have shown that the complex significantly stimulates DNA end joining, binds directly to the DNA substrates, and collaborates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. NONO is implicated in transcriptional regulation. The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates both basal and cAMP-dependent transcriptional activity. Furthermore, NONO binds to an enhancer element in long terminal repeats of endogenous intracisternal A particles (IAPs) and activates transcription. NONO regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. It is vital for the functional organization of GABAergic synapses. NONO plays a specific and essential role in regulating synaptic RNAs and GPHN/gephyrin scaffold structure, through the regulation of GABRA2 transcript. Notably, NONO plays a key role during neuronal differentiation by recruiting TET1 to genomic loci, thereby regulating 5-hydroxymethylcytosine levels. NONO participates in regulating the DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, which serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway.
Gene References Into Functions
- Studies have indicated that NONO is upregulated in human esophageal squamous cell carcinoma (ESCC) tissue samples. Further investigations suggest that NONO plays a significant role in multiple biological aspects of ESCC through the activation of the Akt and Erk1/2 signaling pathways. PMID: 29620226
- Our research has revealed, for the first time, that the expression of p54 was markedly increased in the synovial tissues of rheumatoid arthritis patients. PMID: 29441870
- Our findings unveil a novel mechanism whereby HUR protects NONO from mir320-mediated degradation upon UVC exposure. This identifies a new component within the complex network of players underlying the DNA damage response, adding mir320a to the list of p53-regulated targets upon genotoxic stress. PMID: 27816966
- This study demonstrates that GAPLINC contributes to promoting colorectal cancer invasion via binding to PSF/NONO and partly by stimulating the expression of SNAI2. PMID: 27259250
- We report that l-proline stabilizes purified NONO homodimers, enabling high-quality solution small-angle X-ray structure determination and crystallization. NONO crystallized in the apparent space group P21 with a unique axis (b) of 408.9 A and with evidence of twinning, as indicated by the cumulative intensity distribution L statistic, suggesting the possibility of space group P1. PMID: 27303796
- Our mechanistic dissection reveals that NEAT1 broadly interacts with the NONO-PSF heterodimer as well as numerous other RNA-binding proteins. Multiple RNA segments in NEAT1, including a 'pseudo pri-miRNA' near its 3' end, help attract the Drosha-DGCR8 Microprocessor. PMID: 28846091
- The SFPQ*NONO complex contains an RNA binding domain, and previous research has demonstrated diverse roles in RNA metabolism. Therefore, it is plausible that the additional repair function of NONO, revealed in cell-based assays, could involve RNA interaction. PMID: 27924002
- Exome analysis identified a novel de novo splice-site variant c.1171+1G>T in exon 11 of the NONO gene in a patient with intellectual disability and non-compaction cardiomyopathy. PMID: 27329731
- Case Report: melanotic PEComa of the sinonasal mucosa with NONO-TFE3 fusion. PMID: 28009605
- High expression of P54 is associated with breast cancer. PMID: 27297086
- This study indicates that p54nrb is a powerful molecule involved in regulating cell motility and promotes the migration and invasion of THP1 cells. It is likely involved in the release of inflammatory mediators and the motility of inflammatory cells. PMID: 27108701
- p54(nrb) is a novel regulator of SREBP-1a in the nucleus. Our data suggest that p54(nrb) regulation of SREBP-1a supports the increased cellular demand for lipids required for breast cancer growth. PMID: 26148231
- Our data uncover a new role for NONO in mediating the cellular response to UV-induced DNA damage. PMID: 25893301
- Subnuclear re-localization of SOX10 and p54NRB correlates with a unique neurological phenotype associated with SOX10 missense mutations. PMID: 26060192
- These data suggest that NonO negatively regulates HIV-1 infection in CD4(+) T cells, highlighting the importance of host proteins associated with HIV-1 preintegration complexes in regulating viral replication. PMID: 25769457
- Mutations in NONO have been linked to defects at inhibitory synapses in intellectual disability syndrome. PMID: 26571461
- Our findings suggest that SFPQ.NONO promotes end joining by binding to internal DNA sequences and collaborating with other repair proteins to stabilize a synaptic pre-ligation complex. PMID: 25998385
- Patients with aortic dissection (AD) exhibited significantly decreased expression of P54(nrb) /NonO. The significant correlation between P54(nrb) /NonO and collagen may point to novel insights into collagen metabolism research in AD aorta. PMID: 24720418
- Silencing p54(nrb)/NONO expression in H295R human adrenocortical cells decreases the cells' ability to increase intracellular cAMP production and subsequent cortisol biosynthesis in response to adrenocorticotropin hormone (ACTH) stimulation. PMID: 25605330
- The ability of the SFPQ/NONO complex to form varying protein assemblies, in conjunction with the effect of post-translational modifications of SFPQ modulating mRNA binding, suggests key roles in affecting mRNP dynamics within the cell. PMID: 25605962
- p54 is essential for GC-mediated expression of occludin, claudin-5, and barrier induction. The p54/PSF heterodimer may contribute to normal blood-retinal barrier (BRB) induction in vivo. PMID: 23640037
- We observed the localization of TopBP1 at DNA damage sites as early as 5 s following damage induction, whereas p54(nrb) and PSF localized there after 20 s. PMID: 22213094
- This study describes the crystal structure of the heterodimer of the multidomain conserved region of the Drosophila behavior/human splicing proteins, PSPC1 and NONO. PMID: 22416126
- Our study showed that Rasd1 and NonO interact at the CRE-site of specific target genes. PMID: 21915321
- The crystal of PSPC1-NONO contained one heterodimer in the asymmetric unit and diffracted to 1.9 A resolution using synchrotron radiation. PMID: 22102035
- p54(nrb) interaction with RNA could be selectively modulated by phosphorylation during mitosis. PMID: 21819346
- RVxF motifs play a significant role in controlling the multifunctional properties of p54nrb and PSF in the regulation of gene transcription. PMID: 21566083
- High p54nrb is associated with malignant melanoma. PMID: 21642354
- The NONO/SFPQ heterodimer is involved in the early stages of the DSB response. PMID: 20421735
- The nmt55/p54nrb protein is post-transcriptionally regulated in human breast tumors, leading to reduced expression in ER- tumors and the expression of an amino terminal altered isoform in a subset of ER+ tumors. PMID: 11710964
- PSF and p54nrb bind U5 snRNA, with both the sequence and structure of stem 1b contributing to binding specificity. PSF interacts with p54nrb. PMID: 12403470
- Review article of p54 as a multi-functional nuclear protein. PMID: 12417296
- nmt55 expression is related to hormone-dependency or -independence associated with the androgen receptor. PMID: 12672026
- Results suggest that p54(nrb) functions as a coactivator of androgen receptors, potentiating transcription and possibly splicing. PMID: 12810069
- p54nrb and PSF exhibit properties of key factors mediating INS function and likely define a novel mRNA regulatory pathway that is hijacked by HIV-1. PMID: 12944487
- p54(nrb), which binds the C-terminal domain of the largest subunit of RNAPII, can interact directly with the 5' SS, indicating that these factors may mediate contacts between RNA polymerase II. PMID: 15057275
- The PSF.p54(nrb) complex cooperates with Ku protein to form a functional preligation complex with substrate DNA. PMID: 15590677
- Thus, paraspeckles are the sites where a subset of the total cellular pool of p54nrb is targeted in an RNA Polymerase II-dependent manner. PMID: 16148043
- These data demonstrated that the PSF and p54nrb complex with AR and play a key role in modulating AR-mediated gene transcription. PMID: 17452459
- Identification of PSF, p54(nrb), PTB, and U1A as proteins specifically bound to the COX-2 polyadenylation signal upstream sequence elements. PMID: 17507659
- p54 is present along the length of genes, and small interfering RNA (siRNA)-mediated knockdown leads to defects in XRN2 recruitment and termination. PMID: 17639083
- Findings suggest that the PSF.p54nrb complex is a novel MAP kinase signal-integrating kinases substrate that binds the mRNA for tumor necrosis factor alpha. PMID: 17965020
- At the TERT gene locus in human tumor cells containing a functional SWI/SNF complex, Brm, and possibly BRG1, in concert with p54(nrb), would initiate efficient transcription and could be involved in the subsequent splicing of TERT transcripts. PMID: 18042045
- TORC2 and NONO complex on cAMP-responsive promoters, and NONO acts as a bridge between the CREB/TORC complex and RNA polymerase II. PMID: 18077367
- Co-expression with polypyrimidine tract-binding protein-associated splicing factor (PSF) relocates oncogenic RING finger protein 43 (RNF43) from the nuclear periphery to the nucleoplasm. PMID: 18655028
- p54nrb plays an important role in regulating Sox9 function and the formation of paraspeckle bodies during chondrogenesis. PMID: 18677406
- SOCS3 regulates the action of NonO to suppress MUC8 transcriptional activation. PMID: 18952062
- p54nrb is a transcriptional corepressor of the progesterone receptor that modulates transcription of the labor-associated gene, connexin 43 (Gja1). PMID: 19423654
- We confirm the interactions of eEF1A1, p54(nrb), hnRNP-L, GAPDH, and ASF/SF2 with the right terminal stem-loop domain of HDV genomic RNA in vitro. PMID: 19464723
- NONO is a TORC-interacting protein that is necessary for cAMP-dependent activation of CREB target genes in vivo. TORC2 and NONO complex on cAMP-responsive promoters, and NONO acts as a bridge between the CREB/TORC complex and RNA polymerase II. PMID: 18077367
Database Links
Involvement In Disease
Mental retardation, X-linked, syndromic, 34 (MRXS34)
Subcellular Location
Nucleus. Nucleus, nucleolus. Nucleus speckle. Chromosome. Note=Detected in punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles.
Tissue Specificity
Heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Also found in a number of breast tumor cell lines.
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