Anti-nmt55/p54nrb/NONO Antibody Picoband®

Overview

This antibody is intended for detection of NONO (Non-POU domain-containing octamer-binding protein) in biological samples using common immunoassay formats. It is typically selected based on target identity, species reactivity, clonality/clone information, and detection modality.

Vendor notes: Boster Bio Anti-nmt55/p54nrb/NONO Antibody Picoband® catalog # PB9875. Tested in Flow Cytometry, IF, IHC, ICC, WB applications. This antibody reacts with Human, Mouse, Rat. The brand Picoband indicates this is a premium antibody that guarantees superior quality, high affinity, and strong signals with minimal background in Western blot applications. Only our best-performing antibodies are designated as Picoband, ensuring unmatched performance.

Key elements and design rationale

• Antibody format: Rabbit Polyclonal Rabbit IgG
• Immunogen / epitope context: A synthetic peptide corresponding to a sequence at the N-terminus of human nmt55/p54nrb, identical to the related mouse and rat sequences.
• Molecular weight context: reported MW: 60 kDa; calculated MW: 54232 MW
• Reactivity: Human,Mouse,Rat
• Applications: Flow Cytometry, IF, IHC, ICC, WB

As a polyclonal antibody, the reagent recognizes multiple epitopes on the target, which can improve detection robustness but may increase sensitivity to sample-dependent epitope changes.

Biological background

Non-POU domain-containing octamer-binding protein; Non-POU domain-containing octamer-binding protein. Non-POU domain-containing octamer-binding protein?is a?protein?that in humans is encoded by the?NONO gene. This gene encodes an RNA-binding protein which plays various roles in the nucleus, including transcriptional regulation and RNA splicing. A rearrangement between this gene and the transcription factor E3 gene has been observed in papillary renal cell carcinoma. Alternatively spliced transcript variants have been described. Pseudogenes exist on Chromosomes 2 and 16.? Functional note: 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 ly 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 avtivity. 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. . Reported localization: Nucleus. Nucleus, nucleolus. Nucleus speckle. Detected in punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles. Expression/tissue context: Heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Also found in a number of breast tumor cell lines. .

Research relevance and current trends

• Biochemicals: Researchers commonly examine how NONO (Non-POU domain-containing octamer-binding protein) relates to this theme using model systems and orthogonal readouts.
• Chemical Type: Researchers commonly examine how NONO (Non-POU domain-containing octamer-binding protein) relates to this theme using model systems and orthogonal readouts.
• Signal Transduction: Researchers commonly examine how NONO (Non-POU domain-containing octamer-binding protein) relates to this theme using model systems and orthogonal readouts.

Common research applications

• Western blotting: compare relative NONO (Non-POU domain-containing octamer-binding protein) levels across conditions; band patterns may reflect isoforms and processing.
• IHC/IHC-F: assess spatial distribution of NONO (Non-POU domain-containing octamer-binding protein) across tissue regions and cell types using matched controls.
• IF/ICC: evaluate subcellular localization and co-localization patterns; signal can depend on fixation/permeabilization and epitope accessibility.
• Flow cytometry: quantify target-positive populations and shifts in expression; gating strategy and background staining controls are essential.

Notes for experimental interpretation

• Specificity notes: No cross reactivity with other proteins.
• Cross-reactivity: No cross-reactivity with other proteins.
• Isoforms and PTMs: Apparent size and signal patterns can differ across splice isoforms, proteolytic processing, and post-translational modifications.
• Controls: Include an isotype control (as relevant), no-primary control for imaging, and orthogonal validation such as KD/KO samples when available.

Customization & Add-ons: Can’t find the antibody you need—or require a custom format for your assay? We can help you source the best match or support custom antibody solutions for diverse research needs, including species and isotype selection, conjugations and labeling (e.g., HRP/AP, biotin, fluorophores), purification grade options (Protein A/G, affinity purified), formulation preferences (buffer selection, carrier-free, glycerol-free), custom concentrations and aliquoting, low-endotoxin options for cell-based work, and application-focused QC/validation support (project dependent). Click Talk to a Scientist to submit a request, email us at support@biohippo.com, or explore our Research Services for additional support—our team will follow up with feasibility details and next steps.