A simple and rapid technique for detecting protein phosphorylation using one-dimensional isoelectric focusing gels and immunoblot analysis.

@article{citeulike:2803666, abstract = {We report a technique for detecting protein phosphorylation that involves isoelectric focusing in a vertical mini-gel format followed by immunoblot detection of the target protein. This method uses standard protein gel equipment, allows sensitive detection of protein phosphorylation when phosphospecific antibodies are not available, and provides a stoichiometric measure of phosphorylation. We demonstrate the application of this method for observing phosphorylation of an Arabidopsis thaliana protein in response to biotic stress.}, address = {Department of Biochemistry, University of Missouri-Columbia, Columbia, Missouri, USA.}, author = {Anderson, Jeffrey C C. and Peck, Scott C C. }, citeulike-article-id = {2803666}, doi = {10.1111/j.1365-313X.2008.03550.x}, issn = {1365-313X}, journal = {The Plant journal : for cell and molecular biology}, month = {May}, posted-at = {2008-05-16 03:15:51}, priority = {2}, title = {A simple and rapid technique for detecting protein phosphorylation using one-dimensional isoelectric focusing gels and immunoblot analysis.}, url = {http://dx.doi.org/10.1111/j.1365-313X.2008.03550.x}, year = {2008} }

TY - JOUR ID - citeulike:2803666 L3 - citeulike-article-id:2803666 TI - A simple and rapid technique for detecting protein phosphorylation using one-dimensional isoelectric focusing gels and immunoblot analysis. JF - The Plant journal : for cell and molecular biology AD - Department of Biochemistry, University of Missouri-Columbia, Columbia, Missouri, USA. SN - 1365-313X N2 - We report a technique for detecting protein phosphorylation that involves isoelectric focusing in a vertical mini-gel format followed by immunoblot detection of the target protein. This method uses standard protein gel equipment, allows sensitive detection of protein phosphorylation when phosphospecific antibodies are not available, and provides a stoichiometric measure of phosphorylation. We demonstrate the application of this method for observing phosphorylation of an Arabidopsis thaliana protein in response to biotic stress. AU - Anderson, Jeffrey C AU - Peck, Scott C PY - 2008/05/09/ UR - http://dx.doi.org/10.1111/j.1365-313X.2008.03550.x ER -