Phosphoserine/threonine Antibody

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.

Anti-Phosphoserine/threonine was generated from a panel of phosphoserine and phosphothreonine-containing peptide immunogens designed from human protein sequences.

This antibody was cross-adsorbed to unphosphorylated peptide then Affinity purification using a mix of phosphoserine and phosphothreonine peptides (without carrier) . The antibody detects many serine or threonine phosphorylated proteins by western blot, immunocytochemistry, and ELISA. All peptide sequences used are highly conserved in many species.