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Product Includes Quantity Applications Reactivity MW(kDa) Isotype
NF-κB p65 (L8F6) Mouse mAb 6956 40 µl
H M R Hm Mk Mi B Dg Pg 65 Mouse IgG2b
RelB (C1E4) Rabbit mAb 4922 40 µl
H M R Mk 70 Rabbit IgG
c-Rel Antibody 4727 40 µl
H Mk 78 Rabbit 
NF-κB1 p105/p50 (D7H5M) Rabbit mAb 12540 40 µl
H M 50 Active form. 120 Precursor Rabbit IgG
NF-κB1 p105 Antibody 4717 40 µl
H M R Mk Mi B Pg 120 Rabbit 
NF-κB2 p100/p52 Antibody 4882 40 µl
H M R Mk 52 (mature). 120 (precursor). Rabbit 
NF-κB2 p100/p52 (18D10) Rabbit mAb (Human Specific) 3017 40 µl
H Mk 52 active form. 120 precursor. Rabbit 
NF-κB p65 (D14E12) XP® Rabbit mAb 8242 40 µl
H M R Hm Mk Dg 65 Rabbit IgG
Anti-rabbit IgG, HRP-linked Antibody 7074 100 µl
All Goat 
Anti-mouse IgG, HRP-linked Antibody 7076 100 µl
All Horse 

Product Description

This kit contains reagents to examine total protein levels of the five NF-κB/Rel family members: p65/RelA, RelB, c-Rel, NF-κB1 (p105/p50) and NF-κB2 (p100/p52).


Specificity / Sensitivity

Each antibody in this kit recognizes endogenous levels of its target protein regardless of post-translational modification state such as phosphorylation or acetylation. The NF-κB1 p105/p50 (D7H5M) Rabbit mAb #12540 detects both the precursor protein p105 and its cleavage product p50, while the NF-κB1 p105 Antibody #4717 only detects p105 and will not cross-react with p50. Both the NF-κB2 p100/p52 Antibody #4882 and the NF-κB2 p100/p52 (18D10) Rabbit mAb (Human Specific) #3017 will cross-react with the precursor protein p100 and its cleavage product p52.


Source / Purification

Polyclonal antibodies are produced by immunizing animals with synthetic peptides corresponding to amino acid residues near the carboxy terminus of human c-Rel, at the carboxy terminus of human NF-κB1 p105 and near the amino terminus of human NF-κB2 p100/p52. Antibodies are purified by Protein A and peptide affinity chromatography. Monoclonal antibodies are produced by immunizing animals with synthetic peptides corresponding to amino acid residues near the carboxy terminus of human NF-κB p65, surrounding Ser424 of human RelB, surrounding Gly415 of human NF-κB p105/p50 protein, surrounding Glu498 of human NF-κB p65/RelA protein, and near the amino terminus of human NF-κB2 p100/p52.

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).


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.


Entrez-Gene Id 4790, 5970, 4791, 5966, 5971
Swiss-Prot Acc. P19838, Q04206, Q00653, Q04864, Q01201

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

Vatsyayan J et al. (2008) EMBO Rep 9, 885–90

Busino L et al. (2012) Nat Cell Biol 14, 375–85


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