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 expr...

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Bibliographic Details
Published inHybridoma Vol. 16; no. 3; p. 273
Main Authors Dallas, P B, Yaciuk, P, Moran, E
Format Journal Article
LanguageEnglish
Published United States 01.06.1997
Subjects
Amino Acid Sequence
Animals
Antibodies, Monoclonal - immunology
Blotting, Western
CREB-Binding Protein
Epitopes, B-Lymphocyte - immunology
Molecular Sequence Data
Nuclear Proteins - genetics
Nuclear Proteins - immunology
Restriction Mapping
Trans-Activators
Transcription Factors - genetics
Transcription Factors - immunology
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Summary: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.
ISSN:0272-457X
DOI:10.1089/hyb.1997.16.273