Recombinant Human Non-Pou Domain-Containing Octamer-Binding Protein (NONO) Protein (His-SUMO)

Name: Recombinant Human Non-Pou Domain-Containing Octamer-Binding Protein (NONO) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-06208P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins, Recombinant proteins fall special offers - full-length proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Non-Pou Domain-Containing Octamer-Binding Protein (NONO) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Activity	Not tested.
Uniprotkb	Q15233
Target Symbol	NONO
Synonyms	NonO protein;54 kDa nuclear RNA- and DNA-binding protein;p54nrb;p54nrb;55 kDa nuclear protein;NMT55;DNA-binding p52/p100 complex, 52 kDa subunit
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MQSNKTFNLEKQNHTPRKHHQHHHQQQHHQQQQQQPPPPPIPANGQQASSQNEGLTIDLKNFRKPGEKTFTQRSRLFVGNLPPDITEEEMRKLFEKYGKAGEVFIHKDKGFGFIRLETRTLAEIAKVELDNMPLRGKQLRVRFACHSASLTVRNLPQYVSNELLEEAFSVFGQVERAVVIVDDRGRPSGKGIVEFSGKPAARKALDRCSEGSFLLTTFPRPVTVEPMDQLDDEEGLPEKLVIKNQQFHKEREQPPRFAQPGSFEYEYAMRWKALIEMEKQQQDQVDRNIKEAREKLEMEMEAARHEHQVMLMRQDLMRRQEELRRMEELHNQEVQKRKQLELRQEEERRRREEEMRRQQEEMMRRQQEGFKGTFPDAREQEIRMGQMAMGGAMGINNRGAMPPAPVPAGTPAPPGPATMMPDGTLGLTPPTTERFGQAATMEGIGAIGGTPPAFNRAAPGAEFAPNKRRRY
Expression Range	1-471aa
Protein Length	Full Length
Mol. Weight	67.2 kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	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 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.
Subcellular Location	Nucleus. Nucleus, nucleolus. Nucleus speckle. Chromosome. Note=Detected in punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles.
Database References	HGNC: 7871 OMIM: 300084 KEGG: hsa:4841 STRING: 9606.ENSP00000276079 UniGene: PMID: 29620226 we observed, for the first time, that the expression of p54 was markedly increased in the synovial tissues of rheumatoid arthritis patients. PMID: 29441870 Findings reveal a new mechanism whereby HUR protects NONO from mir320-mediated degradation upon UVC exposure and identify 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 GAPLINC has a role in promoting colorectal cancer invasion via binding to PSF/NONO and partly by stimulating the expression of SNAI2 PMID: 27259250 Here, it is reported that l-proline stabilizes purified NONO homodimers, enabling good-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 Mechanistic dissection reveals that NEAT1 broadly interacts with the NONO-PSF heterodimer as well as many other RNA-binding proteins and that 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 prior work has demonstrated diverse roles in RNA metabolism. It is thus 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 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 The present study indicates that p54nrb is a powerful molecule involved in the regulation of cell motility and promotes the migration and invasion of THP1 cells, and it is more likely to be 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, and the data suggest that p54(nrb) regulation of SREBP-1a supports the increased cellular demand of lipids for breast cancer growth. PMID: 26148231 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 led to defects at inhibitory synapses in intellectual disability syndrome. PMID: 26571461 suggest that SFPQ.NONO promotes end joining by binding to internal DNA sequences and cooperating 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 thinking about collagen metabolism research in AD aorta. PMID: 24720418 silencing p54(nrb)/NONO expression in H295R human adrenocortical cells decreases the ability of the cells 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 affecting mRNP dynamics within the cell. PMID: 25605962 p54 is essential for GC-mediated expression of occludin, claudin-5, and barrier induction, and the p54/PSF heterodimer may contribute to normal blood-retinal barrier (BRB) induction in vivo. PMID: 23640037 Localisation of TopBP1 at DNA damage sites was noticed as early as 5 s following damage induction, whereas p54(nrb) and PSF localised there after 20 s. PMID: 22213094 The crystal structure of the heterodimer of the multidomain conserved region of the Drosophila behavior/human splicing proteins, PSPC1 and NONO, is described. PMID: 22416126 Study showed that Rasd1 and NonO interact at the CRE-site of specific target genes. PMID: 21915321 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 an important 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 NONO/SFPQ heterodimer is involved in the early stage 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 that potentiates transcription and possibly splicing. PMID: 12810069 p54nrb and PSF have 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 indicates 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 a RNA Polymerase II-dependent manner. PMID: 16148043 These data demonstrated that 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 tumour 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 the regulation of 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 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

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.