Key features and details
- Produced recombinantly (animal-free) for high batch-to-batch consistency and long term security of supply
- PE Rabbit monoclonal [E379] to NF-kB p65
- Suitable for: ICC/IF
- Reacts with: Human
- Conjugation: PE. Ex: 488nm, Em: 575nm
Product namePE Anti-NF-kB p65 antibody [E379]
See all NF-kB p65 primary antibodies
DescriptionPE Rabbit monoclonal [E379] to NF-kB p65
ConjugationPE. Ex: 488nm, Em: 575nm
Tested applicationsSuitable for: ICC/IFmore details
Unsuitable for: Flow Cyt
Species reactivityReacts with: Human
Predicted to work with: Mouse
Synthetic peptide within Human NF-kB p65 aa 500 to the C-terminus (C terminal). The exact sequence is proprietary.
Database link: Q04206
- Flow Cyt: HeLa cells. ICC/IF: HeLa cells
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.
Storage instructionsShipped at 4°C. Upon delivery aliquot. Store at +4°C. Do Not Freeze. Store In the Dark.
Storage bufferpH: 7.40
Preservative: 0.02% Sodium azide
Constituents: PBS, 1% BSA
Concentration information loading...
PurityProtein A purified
- Alexa Fluor® 488 Anti-NF-kB p65 antibody [E379] (ab190205)
- Alexa Fluor® 647 Anti-NF-kB p65 antibody [E379] (ab190589)
- Biotin Anti-NF-kB p65 antibody [E379] (ab205823)
- Anti-NF-kB p65 antibody [E379] - BSA and Azide free (ab207297)
- Alexa Fluor® 555 Anti-NF-kB p65 antibody [E379] (ab214634)
- Alexa Fluor® 594 Anti-NF-kB p65 antibody [E379] (ab214846)
- Anti-NF-kB p65 antibody [E379] (ab32536)
Our Abpromise guarantee covers the use of ab208750 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
This product gave a positive signal in HeLa cells fixed with 4% formaldehyde (10 min) and 100% methanol (5 min)
FunctionNF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and p65-c-Rel complexes are transcriptional activators. The NF-kappa-B p65-p65 complex appears to be involved in invasin-mediated activation of IL-8 expression. The inhibitory effect of I-kappa-B upon NF-kappa-B the cytoplasm is exerted primarily through the interaction with p65. p65 shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappa-B complex. Associates with chromatin at the NF-kappa-B promoter region via association with DDX1.
Sequence similaritiesContains 1 RHD (Rel-like) domain.
Domainthe 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
modificationsUbiquitinated, leading to its proteasomal degradation. Degradation is required for termination of NF-kappa-B response.
Monomethylated at Lys-310 by SETD6. Monomethylation at Lys-310 is recognized by the ANK repeats of EHMT1 and promotes the formation of repressed chromatin at target genes, leading to down-regulation of NF-kappa-B transcription factor activity. Phosphorylation at Ser-311 disrupts the interaction with EHMT1 without preventing monomethylation at Lys-310 and relieves the repression of target genes.
Phosphorylation at Ser-311 disrupts the interaction with EHMT1 and promotes transcription factor activity (By similarity). Phosphorylation on Ser-536 stimulates acetylation on Lys-310 and interaction with CBP; the phosphorylated and acetylated forms show enhanced transcriptional activity.
Reversibly acetylated; the acetylation seems to be mediated by CBP, the deacetylation by HDAC3. Acetylation at Lys-122 enhances DNA binding and impairs association with NFKBIA. Acetylation at Lys-310 is required for full transcriptional activity in the absence of effects on DNA binding and NFKBIA association. Acetylation can also lower DNA-binding and results in nuclear export. Interaction with BRMS1 promotes deacetylation of 'Lys-310'.
Cellular localizationNucleus. Cytoplasm. Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B). Colocalized with RELA in the nucleus upon TNF-alpha induction.
- Information by UniProt
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ab208750 staining NF-kB p65 in HeLa 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 ab208750 at 1/500 dilution (Pseudocolored in green) and ab195884, Rat monoclonal to Tubulin (Alexa Fluor® 647), at 1/250 dilution (shown in red). 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 HeLa cells fixed with 100% methanol (5min).
ab208750 has not yet been referenced specifically in any publications.