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Summary: ©2010NatureAmerica,Inc.Allrightsreserved.
NATURE STRUCTURAL & MOLECULAR BIOLOGY ADVANCE ONLINE PUBLICATION 1
R E S OU RC E
An assessment of histone-modification antibody quality
Thea A Egelhofer1,16, Aki Minoda2,3,16, Sarit Klugman4,5,16, Kyungjoon Lee6, Paulina Kolasinska-Zwierz7,8,
Artyom A Alekseyenko9,10, Ming-Sin Cheung7,8, Daniel S Day6, Sarah Gadel11, Andrey A Gorchakov9,10,
Tingting Gu11, Peter V Kharchenko6, Samantha Kuan4,5, Isabel Latorre7,8, Daniela Linder-Basso12,
Ying Luu4,5, Queminh Ngo4,5, Marc Perry13, Andreas Rechtsteiner1, Nicole C Riddle11, Yuri B Schwartz12,
Gregory A Shanower12, Anne Vielle7,8, Julie Ahringer7,8, Sarah C R Elgin11, Mitzi I Kuroda9,10, Vincenzo Pirrotta12,
Bing Ren4,5, Susan Strome1, Peter J Park6, Gary H Karpen2,3, R David Hawkins4,5 & Jason D Lieb14,15
We have tested the specificity and utility of more than 200 antibodies raised against 57 different histone modifications in
Drosophila melanogaster, Caenorhabditis elegans and human cells. Although most antibodies performed well, more than
25% failed specificity tests by dot blot or western blot. Among specific antibodies, more than 20% failed in chromatin
immunoprecipitation experiments. We advise rigorous testing of histone-modification antibodies before use, and we provide
a website for posting new test results (http://compbio.med.harvard.edu/antibodies/).
This December, we celebrate the 100th anniversary of Albrecht Kossel's
1910 Nobel Prize in Physiology or Medicine, which was awarded in
part for his discovery of histone proteins1. In 1964, soon after elucida-
tion of the DNA-RNA-protein `Central Dogma', came strong experi-
mental evidence that histones are acetylated and methylated after
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