Phosphorylation of specific serine or threonine residues is an important post-translational modification for regulating the activity of most proteins. Stimulation of a variety of cell signaling pathways activates the receptor and non-receptor ser/thr kinases that mediate these protein modifications. Antibodies that can detect phosphoserine or phosphothreonine residues are excellent tools for characterizing changes in the post-translational state of a broad range of phosphorylated proteins. Immunoprecipitation of proteins of interest followed by detection of phosphoserine or phosphothreonine using anti-phosphoserine antibody is commonly used to correlate changes in phosphorylation state with alterations in protein activity.
Krishna, R.G. & Wold, F. (1993) Adv Enzymol Rel Areas Mol Biol 67:265.
Hunter T.(1987) Cell. 50(6):823.
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
This kit contains: