A "minimal epitope" anti-protein antibody that recognises a single modified amino acid.
Antibodies that recognise proteins bind to epitopes of varying size, but a grouping of the order of six amino acids, contiguous or not, is regarded as a typical number. By using as immunogen a highly abundant and universal eukaryotic nuclear protein (histone H4) modified in a manner not typical of secreted proteins (acetylation of lysine side chains), antiserum has been raised in rabbits having the single amino acid epsilon-N-acetyl lysine as the recognition epitope. The affinity-purified antibody should be useful for studying the functional role of this modification. The methodology has potential for raising antibodies to other types of post-translationally modified proteins.
Hebbes
T R
TR
Biophysics Laboratories, Portsmouth Polytechnic, U.K.
Turner
C H
CH
Thorne
A W
AW
Crane-Robinson
C
C
D000818:Animals; D000974:Antibodies, Antinuclear / Q000302:isolation & purification; D000917:Antibody Formation; D002843:Chromatin / Q000276:immunology; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000276:immunology*; D006657:Histones / Q000276:immunology*; D015151:Immunoblotting; D008239:Lysine / Q000031:analogs & derivatives* / Q000276:immunology; D011817:Rabbits
D000974:Antibodies, Antinuclear; D002843:Chromatin; D000939:Epitopes; D006657:Histones; C016949:N-epsilon-acetyllysine; D008239:Lysine