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Hunting for serine 276-phosphorylated p65

Anneleen Spooren (UGent) , Krzysztof Kolmus (UGent) , Linda Vermeulen (UGent) , Karlien Van Wesemael (UGent) , Guy Haegeman (UGent) and Sarah Gerlo (UGent)
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Abstract
The transcription factor nuclear factor kappaB (NF-kappa B) is one of the central mediators of inflammatory gene expression. Several posttranslational modifications of NF-kappa B, regulating its transactivation ability, have been described. Especially phosphorylation of the NF-kappa B subunit p65 has been investigated in depth and several commercial phosphospecific antibodies, targeting selected p65 residues, are available. One of the p65 residues, that is subject to phosphorylation by protein kinase A (PKA) as well as by mitogen-stimulated kinase-1 (MSK-1), is the serine at position 276. Here, we have performed a detailed analysis of the performance of the most commonly used commercial anti-P-p65 Ser276 antibodies. Our findings indicate that at least three widely used anti-P-p65 Ser276 antibodies do not detect p65 in vivo via Western Blot, but instead crossreact with PKA-regulated proteins. As PKA is one of the main kinases responsible for phosphorylation of p65 at Ser276, this observation warrants cautious interpretation of data generated using the tested antibodies.
Keywords
INFLAMMATION, SUBUNIT, SEQUENCE, PHOSPHORYLATION, NUCLEAR-FACTOR, TRANSCRIPTIONAL ACTIVITY, NF-KAPPA-B

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Chicago
Spooren, Anneleen, Krzysztof Kolmus, Linda Vermeulen, Karlien Van Wesemael, Guy Haegeman, and Sarah Gerlo. 2010. “Hunting for Serine 276-phosphorylated P65.” Journal of Biomedicine and Biotechnology.
APA
Spooren, A., Kolmus, K., Vermeulen, L., Van Wesemael, K., Haegeman, G., & Gerlo, S. (2010). Hunting for serine 276-phosphorylated p65. JOURNAL OF BIOMEDICINE AND BIOTECHNOLOGY.
Vancouver
1.
Spooren A, Kolmus K, Vermeulen L, Van Wesemael K, Haegeman G, Gerlo S. Hunting for serine 276-phosphorylated p65. JOURNAL OF BIOMEDICINE AND BIOTECHNOLOGY. 2010;
MLA
Spooren, Anneleen, Krzysztof Kolmus, Linda Vermeulen, et al. “Hunting for Serine 276-phosphorylated P65.” JOURNAL OF BIOMEDICINE AND BIOTECHNOLOGY (2010): n. pag. Print.
@article{1150792,
  abstract     = {The transcription factor nuclear factor kappaB (NF-kappa B) is one of the central mediators of inflammatory gene expression. Several posttranslational modifications of NF-kappa B, regulating its transactivation ability, have been described. Especially phosphorylation of the NF-kappa B subunit p65 has been investigated in depth and several commercial phosphospecific antibodies, targeting selected p65 residues, are available. One of the p65 residues, that is subject to phosphorylation by protein kinase A (PKA) as well as by mitogen-stimulated kinase-1 (MSK-1), is the serine at position 276. Here, we have performed a detailed analysis of the performance of the most commonly used commercial anti-P-p65 Ser276 antibodies. Our findings indicate that at least three widely used anti-P-p65 Ser276 antibodies do not detect p65 in vivo via Western Blot, but instead crossreact with PKA-regulated proteins. As PKA is one of the main kinases responsible for phosphorylation of p65 at Ser276, this observation warrants cautious interpretation of data generated using the tested antibodies.},
  articleno    = {275892},
  author       = {Spooren, Anneleen and Kolmus, Krzysztof and Vermeulen, Linda and Van Wesemael, Karlien and Haegeman, Guy and Gerlo, Sarah},
  issn         = {1110-7243},
  journal      = {JOURNAL OF BIOMEDICINE AND BIOTECHNOLOGY},
  keyword      = {INFLAMMATION,SUBUNIT,SEQUENCE,PHOSPHORYLATION,NUCLEAR-FACTOR,TRANSCRIPTIONAL ACTIVITY,NF-KAPPA-B},
  language     = {eng},
  pages        = {9},
  title        = {Hunting for serine 276-phosphorylated p65},
  url          = {http://dx.doi.org/10.1155/2010/275892},
  year         = {2010},
}

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