Key features and details
- Alexa Fluor® 647 Rabbit monoclonal [EPR5270] to nmt55 / p54nrb
- Suitable for: ICC/IF
- Reacts with: Mouse
- Conjugation: Alexa Fluor® 647. Ex: 652nm, Em: 668nm
Product nameAlexa Fluor® 647 Anti-nmt55 / p54nrb antibody [EPR5270]
See all nmt55 / p54nrb primary antibodies
DescriptionAlexa Fluor® 647 Rabbit monoclonal [EPR5270] to nmt55 / p54nrb
ConjugationAlexa Fluor® 647. Ex: 652nm, Em: 668nm
Tested applicationsSuitable for: ICC/IFmore details
Species reactivityReacts with: Mouse
Predicted to work with: Rat, Human
Synthetic peptide within Human nmt55/ p54nrb aa 450 to the C-terminus (C terminal). The exact sequence is proprietary.
Database link: Q15233
- ICC/IF: NIH3T3 cells
This product is a recombinant monoclonal antibody, which offers several advantages including:
- - High batch-to-batch consistency and reproducibility
- - Improved sensitivity and specificity
- - Long-term security of supply
- - Animal-free production
Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C. Avoid freeze / thaw cycle. Store In the Dark.
Storage bufferpH: 7.40
Preservative: 0.02% Sodium azide
Constituents: PBS, 1% BSA, 30% Glycerol
Concentration information loading...
PurityProtein A purified
Our Abpromise guarantee covers the use of ab207375 in the following tested applications.
This product gave a positive signal in NIH3T3 cells fixed with 4% formaldehyde (10 min) and 100% methanol (5 min)
FunctionDNA- 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 (By similarity). Involved in pre-mRNA splicing, probably as an 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. 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 nonhomologous 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 avtivity. NONO binds to an enhancer element in long terminal repeats of endogenous intracisternal A particles (IAPs) and activates transcription.
Tissue specificityHeart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Also found in a number of breast tumor cell lines.
Involvement in diseaseNote=A chromosomal aberration involving NONO may be a cause of papillary renal cell carcinoma (PRCC). Translocation t(X;X)(p11.2;q13.1) with TFE3.
Sequence similaritiesContains 2 RRM (RNA recognition motif) domains.
modificationsThe N-terminus is blocked.
- Information by UniProt
- 52 kDa subunit antibody
- 54 kDa nuclear RNA and DNA binding protein antibody
- 54 kDa nuclear RNA- and DNA-binding protein antibody
ab207375 staining nmt55 / p54nrb in NIH3T3 cells. The cells were fixed with 4% formaldehyde (10 min), permeabilized with 0.1% Triton X-100 for 5 minutes and then blocked with 1% BSA/10% normal goat serum/0.3M glycine in 0.1% PBS-Tween for 1h. The cells were then incubated overnight at +4°C with ab207375 at a 1/100 dilution (shown in red) and ab195887, Mouse monoclonal to alpha Tubulin (Alexa Fluor® 488), at a 1/250 dilution (shown in green). Nuclear DNA was labelled with DAPI (shown in blue).
Image was taken with a confocal microscope (Leica-Microsystems, TCS SP8).
This product also gave a positive signal under the same testing conditions in NIH3T3 cells fixed with 100% methanol (5 min)
ab207375 has not yet been referenced specifically in any publications.