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Protein phosphorylation of serine and threonine residues is critical for the control of protein activity involved in various cellular events. An assortment of Ser/Thr kinases and phosphatases regulate serine and threonine phosphorylation in cell signaling pathways, such as growth factor, cytokine, chemokine, and stress response. Detection of serine and threonine phosphorylation can generally be monitored by antibodies that detect phosphoserine and phosphothreonine. Our clone 19 antibody specifically recognizes phosphoserine modifications on peptides in ELISA, while our clone 22a detects both phosphoserine and phosphothreonine modifications on peptides in ELISA. These antibodies are reported to be useful for Western blot, flow cytometry, and microscopy detection of phosphoserine and phosphothreonine levels.Immunofluorescence, Western Blotting
