Anti-NF-kB p65 (phospho S536) antibody (ab28856)

Overview

  • Product nameAnti-NF-kB p65 (phospho S536) antibody
    See all NF-kB p65 primary antibodies
  • Description
    Rabbit polyclonal to NF-kB p65 (phospho S536)
  • SpecificityNF-kappaB p65 (Phospho-Ser536) Antibody detects endogenous levels of NF-kappaB p65 only when phosphorylated at serine536
  • Tested applicationsWB, IHC-P, ELISA, IPmore details
  • Species reactivity
    Reacts with: Mouse, Rat, Human
  • Immunogen

    Synthetic peptide corresponding to NF-kB p65 (C terminal) (phospho S536).

  • Positive control
    • Human breast carcinoma,K562 cells,COLO cells

Properties

Applications

Our Abpromise guarantee covers the use of ab28856 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

Application Abreviews Notes
WB 1/500 - 1/1000. Predicted molecular weight: 60 kDa.
IHC-P 1/50 - 1/100.
ELISA 1/10000.
IP Use at an assay dependent concentration.

Target

  • 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.
  • Post-translational
    modifications
    Ubiquitinated, 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
  • Database links
  • Alternative names
    • Avian reticuloendotheliosis viral (v rel) oncogene homolog A antibody
    • MGC131774 antibody
    • NF kappa B p65delta3 antibody
    • NFKB 3 antibody
    • NFKB3 antibody
    • Nuclear Factor NF Kappa B p65 Subunit antibody
    • Nuclear factor NF-kappa-B p65 subunit antibody
    • Nuclear factor of kappa light polypeptide gene enhancer in B cells 3 antibody
    • Nuclear Factor Of Kappa Light Polypeptide Gene Enhancer In B Cells antibody
    • Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3 antibody
    • OTTHUMP00000233473 antibody
    • OTTHUMP00000233474 antibody
    • OTTHUMP00000233475 antibody
    • OTTHUMP00000233476 antibody
    • OTTHUMP00000233900 antibody
    • p65 antibody
    • p65 NF kappaB antibody
    • p65 NFkB antibody
    • RELA antibody
    • TF65_HUMAN antibody
    • Transcription Factor p65 antibody
    • v rel avian reticuloendotheliosis viral oncogene homolog A (nuclear factor of kappa light polypeptide gene enhancer in B cells 3 (p65)) antibody
    • V Rel Avian Reticuloendotheliosis Viral Oncogene Homolog A antibody
    • v rel reticuloendotheliosis viral oncogene homolog A (avian) antibody
    • V rel reticuloendotheliosis viral oncogene homolog A, nuclear factor of kappa light polypeptide gene enhancer in B cells 3, p65 antibody
    • v-rel reticuloendotheliosis viral oncogene homolog A antibody
    see all

Anti-NF-kB p65 (phospho S536) antibody images

  • Paraffin embedded human breast carcinoma stained with ab28856. Left: ab28856, Right: same antibody preincubated with the corresponding synthesized phosphopeptide.

  • Lanes 1 - 2 : Anti-NF-kB p65 (phospho S536) antibody (ab28856)
    Lane 3 :

    Lane 1 : K562 cells
    Lane 2 : COLO cells
    Lane 3 : Synthesized peptide


    Predicted band size : 60 kDa

References for Anti-NF-kB p65 (phospho S536) antibody (ab28856)

This product has been referenced in:
  • Song Z  et al. CD40 Is Essential in the Upregulation of TRAF Proteins and NF-KappaB-Dependent Proinflammatory Gene Expression after Arterial Injury. PLoS One 6:e23239 (2011). IHC-P ; Mouse . Read more (PubMed: 21876738) »
  • Lewander A  et al. NF-?B p65 phosphorylated at serine-536 is an independent prognostic factor in Swedish colorectal cancer patients. Int J Colorectal Dis : (2011). IHC-P ; Human . Read more (PubMed: 22102084) »

See all 2 Publications for this product

Product Wall

Thank you for contacting us. Because we carry over 90,000 products, it isn't feasible for us to keep small sample sizes of our products.

We are happy to reassure our customers that all of our products are covered by our Abpromise, which guaran...

Read More

DISCOUNT CODE: **********
Expiration date: *************

I am very pleased to hear you would like to accept our offer and test ab28856 inIHC-Fr. This code will give you: 1 free PRIMARY ANTIBODY before the expiration date. To redeem this...

Read More

Thank you very much for your interest in 28856 & ab51059.

To our knowledge, 28856 & ab51059 have not been tested in IHC-Fr. Therefore, I can offer a discount off a future purchase if you buy 28856 & ab51059 now, test it in IHC-Fr...

Read More

DISCOUNT CODE: *** Expiration date: April 19th, 2012 I am very pleased to hear you would like to accept our offer and test ab28856 in sheep. This code will give you 1 free primary antibody before the expiration date. To redeem this offer, please submit...

Read More

Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"