NONO Antibody (YA1406)
(Synonyms: P54; NMT55; NRB54; P54NRB)Based on 1 Customer Validation
NONO Antibody (YA1406) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to NONO.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-F, IHC-P, ICC/IF
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in 50mM Tris-Glycine(pH 7.4), 0.15M NaCl, 40% Glycerol, 0.01% Sodium azide and 0.05% BSA
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Conjugation:
Non-conjugated
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
|---|---|---|---|
| Dilution Ratio | 1:1000-1:5000 | 1:200-1:500 | 1:500-1:2000 |
Product Details
NONO Antibody (YA1406) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to NONO.
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Host Rabbit
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Clonality Recombinant,Monoclonal
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Species ReactivityHuman, Mouse, Rat
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Observed Molecular WeightObserved band size: 62 kDaNote: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 54 kDa
Entrez Gene: 4841 Human ; 53610 Mouse ; 317259 Rat
SwissProt: Q15233 Human ; Q99K48 Mouse ; Q5FVM4 Rat
OMIM: 300967 Human
A synthetic peptide of human NMT55/p54nrb
Endogenous
Affinity Purified
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in 50mM Tris-Glycine(pH 7.4), 0.15M NaCl, 40% Glycerol, 0.01% Sodium azide and 0.05% BSA
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Concentration
Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
NONO is a DNA- and RNA binding protein, involved in several nuclear processes. Binds the conventional octamer sequence in double-stranded DNA. Also binds single-stranded DNA and RNA at a site independent of the duplex site. Involved in pre-mRNA splicing, probably as a heterodimer with SFPQ. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. Together with PSPC1, required for the formation of nuclear paraspeckles. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1. The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends. In vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. NONO is involved in transcriptional regulation. The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity. NONO binds to an enhancer element in long terminal repeats of endogenous intracisternal A particles (IAPs) and activates transcription. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer. Important for the functional organization of GABAergic synapses. Plays a specific and important role in the regulation of synaptic RNAs and GPHN/gephyrin scaffold structure, through the regulation of GABRA2 transcript. Plays a key role during neuronal differentiation by recruiting TET1 to genomic loci and thereby regulating 5-hydroxymethylcytosine levels. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway. Promotes activation of the cGAS-STING pathway in response to HIV-2 infection: acts by interacting with HIV-2 Capsid protein p24, thereby promoting detection of viral DNA by CGAS, leading to CGAS-mediated inmmune activation. In contrast, the weak interaction with HIV-1 Capsid protein p24 does not allow activation of the cGAS-STING pathway[1][2][3][4][5][6][7][8][9].
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Subcellular Localization
Nucleus; Nucleus, nucleolus; Nucleus speckle; Chromosome
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Expression
Tissue_specificity:Heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Also found in a number of breast tumor cell lines -
Isoforms & Post-Translational Modification
Q15233 has 2 isomers: Q15233-1: 54232 Da (predicted); Q15233-2: 43866 Da (predicted).
The N-terminus is blocked -
Subunit
Monomer and component of the SFPQ-NONO complex, which is probably a heterotetramer of two 52 kDa (NONO) and two 100 kDa (SFPQ) subunits (PubMed:15590677, PubMed:8439294). NONO is a component of spliceosome and U5.4/6 snRNP complexes (PubMed:12403470). Interacts with CPNE4 (via VWFA domain) (By similarity). Forms heterodimers with PSPC1; this involves formation of a coiled coil domain by helices from both proteins (PubMed:16148043, PubMed:22416126). Part of complex consisting of SFPQ, NONO and MATR3 (PubMed:11525732). Part of a complex consisting of SFPQ, NONO and NR5A1 (PubMed:11897684). Part of a complex consisting of SFPQ, NONO and TOP1 (PubMed:9756848). Interacts with SPI1 and SPIB (By similarity). Interacts with RNF43 (PubMed:18655028). Interacts with PER1 and PER2 (By similarity). Part of the HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA (PubMed:28712728). Interacts (via second RRM domain) with WASL; the interaction is direct (PubMed:16767080). Component of a multiprotein complex with WASL and SFPQ (PubMed:16767080). Interacts with ERCC6 (PubMed:26030138). Interacts (via DNA-binding domain) with TET1 (By similarity)
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SwissProt ID
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Synonyms
P54; NMT55; NRB54; P54NRB
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Research Field
Epigenetics and Nuclear Signaling
Documentation
[1]. Zhang Z, et al. The fate of dsRNA in the nucleus: a p54(nrb)-containing complex mediates the nuclear retention of promiscuously A-to-I edited RNAs. Cell. 2001 Aug 24;106(4):465-75. [Content Brief]
[2]. Peng R, et al. PSF and p54nrb bind a conserved stem in U5 snRNA. RNA. 2002 Oct;8(10):1334-47. [Content Brief]
[3]. Mircsof D, et al. Mutations in NONO lead to syndromic intellectual disability and inhibitory synaptic defects. Nat Neurosci. 2015 Dec;18(12):1731-6. [Content Brief]
[4]. Passon DM, et al. Structure of the heterodimer of human NONO and paraspeckle protein component 1 and analysis of its role in subnuclear body formation. Proc Natl Acad Sci U S A. 2012 Mar 27;109(13):4846-50. [Content Brief]
[5]. Straub T, et al. PSF/p54(nrb) stimulates "jumping" of DNA topoisomerase I between separate DNA helices. Biochemistry. 2000 Jun 27;39(25):7552-8. [Content Brief]
[6]. Bladen CL, et al. Identification of the polypyrimidine tract binding protein-associated splicing factor.p54(nrb) complex as a candidate DNA double-strand break rejoining factor. J Biol Chem. 2005 Feb 18;280(7):5205-10. [Content Brief]
[7]. Sewer MB, et al. Transcriptional activation of human CYP17 in H295R adrenocortical cells depends on complex formation among p54(nrb)/NonO, protein-associated splicing factor, and SF-1, a complex that also participates in repression of transcription. Endocrinology. 2002 Apr;143(4):1280-90. [Content Brief]
[8]. Morchikh M, et al. HEXIM1 and NEAT1 Long Non-coding RNA Form a Multi-subunit Complex that Regulates DNA-Mediated Innate Immune Response. Mol Cell. 2017 Aug 3;67(3):387-399.e5. [Content Brief]
[9]. Lahaye X, et al. NONO Detects the Nuclear HIV Capsid to Promote cGAS-Mediated Innate Immune Activation. Cell. 2018 Oct 4;175(2):488-501.e22. [Content Brief]