{"product_id":"recombinant-human-non-pou-domain-containing-octamer-binding-protein-nono-bhp10506325","title":"Recombinant Human Non-POU domain-containing octamer-binding protein (NONO)","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\u003cp\u003eThis Recombinant Protein provides recombinant \u003cstrong\u003eNONO\u003c\/strong\u003e from Homo sapiens (Human), produced in E.coli (region 1-471aa). It is commonly used as a defined reagent for assay development, binding studies, and mechanistic research (RUO).\u003c\/p\u003e\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eRegion:\u003c\/strong\u003e 1-471aa (domain boundaries can affect binding\/activity readouts).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eExpression host:\u003c\/strong\u003e E.coli (may differ from native PTMs\/processing).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTag(s):\u003c\/strong\u003e His (supports purification\/detection; consider tag effects in controls).\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eBiological background\u003c\/h2\u003e\u003cp\u003eAlso reported as 54 kDa nuclear RNA- and DNA-binding protein (55 kDa nuclear protein) (DNA-binding p52\/p100 complex, 52 kDa subunit) (NMT55) (p54(nrb)) () (p54nrb) (NRB54). 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-ARNTL\/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 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.\u003c\/p\u003e\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\u003cul\u003e\u003cli\u003eUse of recombinant standards to improve assay calibration and cross-study comparability.\u003c\/li\u003e\u003c\/ul\u003e\u003cp\u003eDNA- 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-ARNTL\/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 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\u003c\/p\u003e\u003ch2\u003eCommon research applications\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003eStandard curve or spike-in reference for quantitative assays involving NONO\u003c\/li\u003e\n\u003cli\u003eBinding and specificity benchmarking for detection reagents (conceptual)\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003eRecombinant constructs may not capture all native isoforms or PTMs.\u003c\/li\u003e\n\u003cli\u003eConsider tag- or host-related effects when interpreting binding or activity.\u003c\/li\u003e\n\u003cli\u003eUse appropriate blanks and matrix\/control concepts to separate signal from background.\u003c\/li\u003e\n\u003c\/ul\u003e\u003c!-- Sources (internal): - UniProtKB Q15233 — UniProt — https:\/\/www.uniprot.org\/uniprotkb\/Q15233 - NCBI Gene search: NONO — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=NONO - Ensembl search: NONO — Ensembl — https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=NONO - Reactome Pathway Browser — Reactome — https:\/\/reactome.org\/ - NCBI Bookshelf — NCBI — https:\/\/www.ncbi.nlm.nih.gov\/books\/ --\u003e","brand":"CUSABIO TECHNOLOGY LLC","offers":[{"title":"1 mg","offer_id":53053381050733,"sku":"CSB-EP624018HUb0-1MG","price":2466.0,"currency_code":"USD","in_stock":true},{"title":"100 ug","offer_id":53053483876717,"sku":"CSB-EP624018HUb0-100UG","price":729.0,"currency_code":"USD","in_stock":true},{"title":"20 ug","offer_id":53053483909485,"sku":"CSB-EP624018HUb0-20UG","price":388.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/CSB-EP624018HUb0-SDS.jpg?v=1772177559","url":"https:\/\/www.ebiohippo.com\/products\/recombinant-human-non-pou-domain-containing-octamer-binding-protein-nono-bhp10506325","provider":"BioHippo","version":"1.0","type":"link"}