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Product Includes Quantity Applications Reactivity MW(kDa) Isotype
Phospho-NF-κB p65 (Ser536) (93H1) Rabbit mAb 3033 40 µl
Western Blotting Immunoprecipitation Immunofluorescence Flow Cytometry
H M R Hm Mk Pg 65 Rabbit IgG
Acetyl-NF-κB p65 (Lys310) (D2S3J) Rabbit mAb 12629 40 µl
Western Blotting Immunoprecipitation
H M 65 Rabbit IgG
NF-κB p65 (L8F6) Mouse mAb 6956 40 µl
Western Blotting Immunoprecipitation Immunohistochemistry Immunofluorescence Flow Cytometry Chromatin Immunoprecipitation
H M R Hm Mk Mi B Dg Pg 65 Mouse IgG2b
NF-κB p65 (D14E12) XP® Rabbit mAb 8242 40 µl
Western Blotting Immunoprecipitation Immunohistochemistry Immunofluorescence Flow Cytometry Chromatin Immunoprecipitation
H M R Hm Mk Dg 65 Rabbit IgG
Phospho-NF-κB p65 (Ser468) Antibody 3039 40 µl
Western Blotting Immunoprecipitation
H M R 65 Rabbit 
Anti-rabbit IgG, HRP-linked Antibody 7074 100 µl
Western Blotting
All Goat 
Anti-mouse IgG, HRP-linked Antibody 7076 100 µl
Western Blotting
All Horse 

Product Description

The NF-κB p65 Antibody Sampler Kit contains reagents to examine NF-κB p65/RelA phosphorylation at Ser468 and Ser536; acetylation at Lys310; and total p65 levels.


Specificity / Sensitivity

The total NF-κB p65 antibodies recognize endogenous levels of p65 regardless of post-translational modification state such as phosphorylation or acetylation. The phospho-NF-κB p65 antibodies recognize endogenous levels of p65 only when phosphorylated at their indicated target residues. The Acetyl-NF-κB p65 (Lys310) (D2S3J) Rabbit mAb recognizes transfected levels of p65 only when acetylated at Lys310.


Source / Purification

The NF-κB p65 (L8F6) Mouse mAb was produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human NF-κB p65. The Acetyl-NF-κB p65 (Lys310) (D2S3J) Rabbit mAb was produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Lys310 of human NF-κB p65 protein. The NF-κB p65 Antibody was produced by immunizing rabbits with a synthetic peptide corresponding to amino acids surrounding Glu498 of human NF-κB p65. The phospho-specific antibodies were produced by immunizing rabbits with synthetic phosphopeptides corresponding to amino acids surrounding the indicated target residues of human NF-κB p65. Polyclonal antibodies were purified by protein A and peptide affinity chromatography.

Transcription factors of the nuclear factor κB (NF-κB)/Rel family play a pivotal role in inflammatory and immune responses (1,2). There are five family members in mammals: RelA, c-Rel, RelB, NF-κB1 (p105/p50), and NF-κB2 (p100/p52). Both p105 and p100 are proteolytically processed by the proteasome to produce p50 and p52, respectively. Rel proteins bind p50 and p52 to form dimeric complexes that bind DNA and regulate transcription. In unstimulated cells, NF-κB is sequestered in the cytoplasm by IκB inhibitory proteins (3-5). NF-κB-activating agents can induce the phosphorylation of IκB proteins, targeting them for rapid degradation through the ubiquitin-proteasome pathway and releasing NF-κB to enter the nucleus where it regulates gene expression (6-8). NIK and IKKα (IKK1) regulate the phosphorylation and processing of NF-κB2 (p100) to produce p52, which translocates to the nucleus (9-11).


RelA/p65 is a subunit of the NF-κB transcription complex, which plays a crucial role in inflammatory and immune responses. The complex is composed of various homodimeric and heterodimeric Rel family member combinations, the activity of which is modulated by post-translational modifications including phosphorylation and acetylation. p65 phosphorylation by PKA and/or MSK1 at Ser276 allows for increased interaction with the transcriptional coactivator p300/CBP to enhance transcriptional activity. NF-κB dimer assembly with IκB, as well as its DNA binding and transcriptional activities, are regulated by p300/CBP acetyltransferases that principally target Lys218, Lys221 and Lys310 (12-14). This process is reciprocally regulated by histone deacetylases (HDACs); several HDAC inhibitors have been shown to activate NF-κB (12-14). T-cell co-stimulation and Calyculin A have both been shown to increase Ser468 phosphorylation (15,16). IKKβ (but not IKKα) and GSK-3β both target this site (16,17), which appears to have a negative regulatory role not involving inhibition of nuclear translocation after TNF-α or IL-1β stimulation (17). p65 phosphorylation at Ser536 regulates activation, nuclear localization, protein-protein interactions, transcriptional activity, and apoptosis (18-22).


1.  Baeuerle, P.A. and Henkel, T. (1994) Annu Rev Immunol 12, 141-79.

2.  Baeuerle, P.A. and Baltimore, D. (1996) Cell 87, 13-20.

3.  Haskill, S. et al. (1991) Cell 65, 1281-9.

4.  Thompson, J.E. et al. (1995) Cell 80, 573-82.

5.  Whiteside, S.T. et al. (1997) EMBO J 16, 1413-26.

6.  Traenckner, E.B. et al. (1995) EMBO J 14, 2876-83.

7.  Scherer, D.C. et al. (1995) Proc Natl Acad Sci USA 92, 11259-63.

8.  Chen, Z.J. et al. (1996) Cell 84, 853-62.

9.  Senftleben, U. et al. (2001) Science 293, 1495-9.

10.  Coope, H.J. et al. (2002) EMBO J 21, 5375-85.

11.  Xiao, G. et al. (2001) Mol Cell 7, 401-9.

12.  Mattioli I et al. (2004) Blood 104, 3302–4

13.  Buss H et al. (2004) J Biol Chem 279, 49571–4

14.  Schwabe RF and Sakurai H (2005) FASEB J 19, 1758–60

15.  Doyle SL et al. (2005) J Biol Chem 280, 23496–501

16.  Buss H et al. (2004) J Biol Chem 279, 55633–43

17.  Mattioli, I. et al. (2004) J Immunol 172, 6336-44.

18.  Ashburner, B.P. et al. (2001) Mol Cell Biol 21, 7065-77.

19.  Mayo, M.W. et al. (2003) J Biol Chem 278, 18980-9.

20.  Chen, L.F. et al. (2002) EMBO J 21, 6539-48.

21.  Sasaki, C.Y. et al. (2005) J Biol Chem 280, 34538-47.

22.  Bae, J.S. et al. (2003) Biochem Biophys Res Commun 305, 1094-8.


Entrez-Gene Id 5970
Swiss-Prot Acc. Q04206

Protein Specific References

Fujita F et al. (2003) Mol Cell Biol 23, 7780–93

Ryo A et al. (2003) Mol Cell 12, 1413–26

Sakurai H et al. (2003) J Biol Chem 278, 36916–23

Mattioli I et al. (2004) Blood 104, 3302–4

Buss H et al. (2004) J Biol Chem 279, 55633–43

Hu J et al. (2004) Carcinogenesis 25, 1991–2003

Buss H et al. (2004) J Biol Chem 279, 49571–4

Doyle SL et al. (2005) J Biol Chem 280, 23496–501

Schwabe RF and Sakurai H (2005) FASEB J 19, 1758–60

Sancho R et al. (2005) J Immunol 175, 3990–9

Wang J et al. (2007) Cancer Cell 12, 239–51

Saha RN et al. (2007) J Immunol 179, 7101–9

Liu P et al. (2007) J Virol 81, 1401–11

Singh M et al. (2007) Chembiochem 8, 1308–16

Buerki C et al. (2008) Nucleic Acids Res 36, 1665–80

Dai Y et al. (2008) Clin Cancer Res 14, 549–58

Lee H et al. (2009) Cancer Cell 15, 283–93

Fan Y et al. (2009) J Biol Chem 284, 29290–7

Nihira K et al. (2010) Cell Death Differ 17, 689–98

Moreno R et al. (2010) Nucleic Acids Res 38, 6029–44

Jiao J et al. (2010) J Virol 84, 7668–74

O'Shea JM and Perkins ND (2010) Biochem J 426, 345–54

Rovillain E et al. (2011) Oncogene 30, 2356–66

Spiller SE et al. (2011) BMC Cancer 11, 136

Breitenstein A et al. (2011) Cardiovasc Res 89, 464–72

Clavijo PE and Frauwirth KA (2012) J Immunol 188, 1213–21

Pringle LM et al. (2012) Oncogene 31, 3525–35

Ziesché E et al. (2013) Nucleic Acids Res 41, 90–109

Fujita F et al. (2003) Mol Cell Biol 23, 7780–93

Ryo A et al. (2003) Mol Cell 12, 1413–26

Sakurai H et al. (2003) J Biol Chem 278, 36916–23

Mattioli I et al. (2004) Blood 104, 3302–4

Buss H et al. (2004) J Biol Chem 279, 55633–43

Hu J et al. (2004) Carcinogenesis 25, 1991–2003

Buss H et al. (2004) J Biol Chem 279, 49571–4

Doyle SL et al. (2005) J Biol Chem 280, 23496–501

Schwabe RF and Sakurai H (2005) FASEB J 19, 1758–60

Sancho R et al. (2005) J Immunol 175, 3990–9

Wang J et al. (2007) Cancer Cell 12, 239–51

Saha RN et al. (2007) J Immunol 179, 7101–9

Liu P et al. (2007) J Virol 81, 1401–11

Singh M et al. (2007) Chembiochem 8, 1308–16

Buerki C et al. (2008) Nucleic Acids Res 36, 1665–80

Dai Y et al. (2008) Clin Cancer Res 14, 549–58

Lee H et al. (2009) Cancer Cell 15, 283–93

Fan Y et al. (2009) J Biol Chem 284, 29290–7

Nihira K et al. (2010) Cell Death Differ 17, 689–98

Moreno R et al. (2010) Nucleic Acids Res 38, 6029–44

Jiao J et al. (2010) J Virol 84, 7668–74

O'Shea JM and Perkins ND (2010) Biochem J 426, 345–54

Rovillain E et al. (2011) Oncogene 30, 2356–66

Spiller SE et al. (2011) BMC Cancer 11, 136

Breitenstein A et al. (2011) Cardiovasc Res 89, 464–72

Clavijo PE and Frauwirth KA (2012) J Immunol 188, 1213–21

Pringle LM et al. (2012) Oncogene 31, 3525–35

Ziesché E et al. (2013) Nucleic Acids Res 41, 90–109


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U.S. Patent No. 5,675,063.