Monoclonal antibody NM11 recognizes a C-terminal epitope shared by p300 and CBP.
The epitope recognized by the monoclonal antibody NM11, previously shown to recognize both CBP and p300, has been mapped here to the C-terminal third of p300 and CBP by Western analysis of p300 and CBP prokaryotic fusion proteins. More precise epitope mapping, carried out by screening a plasmid expression library derived from small randomly generated CBP cDNA fragments localizes the NM11 epitope to a 21 amino acid stretch spanning amino acids 2071-2091 near the CBP C-terminus. CBP and p300 differ by three noncontiguous residues within this 21 amino acid region, a difference that does not detectably affect the reactivity of NM11.
Dallas
P B
PB
Fels Institute for Cancer Research and Molecular Biology, Temple University School of Medicine, Philadelphia, Pennsylvania 19140, USA.
Yaciuk
P
P
Moran
E
E
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology*; D015153:Blotting, Western; D050882:CREB-Binding Protein; D018985:Epitopes, B-Lymphocyte / Q000276:immunology*; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000235:genetics / Q000276:immunology*; D015183:Restriction Mapping; D015534:Trans-Activators; D014157:Transcription Factors / Q000235:genetics / Q000276:immunology*
D000911:Antibodies, Monoclonal; D018985:Epitopes, B-Lymphocyte; D009687:Nuclear Proteins; D015534:Trans-Activators; D014157:Transcription Factors; D050882:CREB-Binding Protein