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J Biotechnol. 2011 Feb 10;151(3):251-4. doi: 10.1016/j.jbiotec.2010.12.013. Epub 2010 Dec 23.

Characterization of a rabbit polyclonal antibody against threonine-AMPylation.

Author information

1
Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.

Abstract

An antibody against the posttranslational modification AMPylation was produced using a peptide corresponding to human Rac1 switch I region with AMPylated threonine-35 residue as an antigen. The resulting rabbit antiserum was tested for its abilities to recognize AMPylated proteins by western blot and immunoprecipitation. The antiserum is highly specific for threonine-AMPylated proteins and weakly recognizes tyrosine-AMPylated proteins. Depletion of serum with modified protein abolished its activity against tyrosine-AMPylated proteins. The antiserum also recognized native proteins with modification in an immunoprecipitation experiment. Interactions of the antiserum could be inhibited by competition with AMP but not with GMP or UMP. This antiserum had potential utility for the identification of unknown AMPylated proteins.

PMID:
21185336
PMCID:
PMC4391625
DOI:
10.1016/j.jbiotec.2010.12.013
[Indexed for MEDLINE]
Free PMC Article

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