Description_x000D_ Specificity_x000D_ By ELISA and dot blot, the antibody reacts specifically with phosphorylated serine, both as free amino acid or conjugated to carriers such as BSA or KLH. No cross-reactivity is observed with non-phosphorylated serine, phosphothreonine, phosphotyrosine, AMP or ATP. This antibody has been used in immunoblotting for the localization of some phosphoserine-containing proteins. Certain proteins known to contain phosphorylated serine may not be recognized by this antibody due to steric hindrance of the recognition site._x000D_ Immunogen_x000D_ phosphoserine conjugated to Keyhole Limpet Hemocyanin (KLH)._x000D_ Application_x000D_ The antibody has been used for the detection of some phosphoserine containing proteins using immunoblotting and dot blotting._x000D_ Physical form_x000D_ Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide._x000D_ Disclaimer_x000D_ Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals._x000D_ Biochem/physiol Actions_x000D_ Protein phosphorylation and dephosphorylation are basic signaling mechanisms that modify protein function in eukaryotic cells. Phosphorylation is a rare posttranslational event in normal tissues, however, the abundance of phosphorylated cellular proteins increases several folds following various activation processes. The main amino acids that are phosphorylated are tyrosine, serine, or threonine (pTyr/pSer/pThr), each having specific kinases that phosphorylate them and specific phosphatases that dephosphorylate them. Mono and polyclonal antibodies directed against phosphorylated residues were generated and found useful as analytical and preparative tools by enabling the identification, quantification, and immunoaffinity isolation of phosphorylated cellular proteins.