Anti-phospho-Myosin (Ser19/Ser20)

This affinity purified antibody is directed against the regulatory light chain of smooth and non-muscle myosin. The antibody is phosphospecific and detects monophosphorylated and diphosphorylated forms of the protein. The product was affinity purified from monospecific antiserum by immunoaffinity purification. Antiserum was first purified against the phosphorylated form of the immunizing peptide. The resultant affinity purified antibody was then cross-adsorbed against the non-phosphorylated form of the immunizing peptide. This phosphospecific polyclonal antibody is specific for the phosphorylated pS19/pS20 form of the protein, depending on the source origin of the protein. Reactivity with non-phosphorylated myosin light chain is less than 1% by ELISA. Cross reactivity is expected with myosin light chain from human and mouse. Reactivity with the protein from other species has not been determined. However, the sequence of the immunogen is nearly identical in mammalian and avian species. BLAST search analysis was used to determine that the smooth and non-muscle forms of myosin regulatory light chain have identical sequences. Cross reactivity is expected. Protein function: Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Implicated in cytokinesis, receptor capping, and cell locomotion. [The UniProt Consortium]